Source 1primary paper2017Photosynthesis Research
Toolkit/light-harvesting complex II
light-harvesting complex II
Also known as: chlorophyll a/b light-harvesting complex II, LHCII, major photosynthetic antenna complex of plants
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Light-harvesting complex II (LHCII) is the major chlorophyll a/b-binding photosynthetic antenna complex of plants that has been studied in isolated native and recombinant forms. The cited literature indicates that light induces reversible conformational changes in LHCII that expose its N-terminal phosphorylation site and can also promote formation of dimeric LHCII states with distinct chlorophyll excitation-quenching properties.
Usefulness & Problems
Why this is useful
LHCII is useful as a naturally light-responsive protein domain for studying how illumination alters protein conformation, substrate accessibility, and oligomeric state in a photosynthetic membrane protein. The cited work supports its use as a model for light-regulated phosphorylation and photoprotective excitation quenching, but does not establish it as a broadly engineered optogenetic actuator.
Source:
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
Problem solved
The cited studies address how light can regulate thylakoid protein phosphorylation at the substrate level by exposing the LHCII phosphorylation site through reversible conformational change. They also address how high light can induce LHCII dimerization into organizational states associated with altered excitation quenching, a process discussed as a potential component of plant photoprotection.
Problem links
Need conditional control of signaling activity
DerivedLight-harvesting complex II (LHCII) is the major chlorophyll a/b-binding photosynthetic antenna complex of plants and has been studied in isolated native and recombinant forms. The cited literature shows that light induces reversible conformational changes in LHCII that expose its N-terminal phosphorylation site and can also promote formation of dimeric LHCII states with distinct quenching properties.
Need conditional recombination or state switching
DerivedLight-harvesting complex II (LHCII) is the major chlorophyll a/b-binding photosynthetic antenna complex of plants and has been studied in isolated native and recombinant forms. The cited literature shows that light induces reversible conformational changes in LHCII that expose its N-terminal phosphorylation site and can also promote formation of dimeric LHCII states with distinct quenching properties.
Need precise spatiotemporal control with light input
DerivedLight-harvesting complex II (LHCII) is the major chlorophyll a/b-binding photosynthetic antenna complex of plants and has been studied in isolated native and recombinant forms. The cited literature shows that light induces reversible conformational changes in LHCII that expose its N-terminal phosphorylation site and can also promote formation of dimeric LHCII states with distinct quenching properties.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
Conformational Uncagingexcitation quenchingexcitation quenchinglight-induced conformational switchinglight-induced conformational switchinglight-induced oligomerization/dimerizationlight-induced oligomerization/dimerizationPhotocleavagesubstrate accessibility uncagingsubstrate accessibility uncagingTechniques
No technique tags yet.
Target processes
recombinationsignalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: cleavageswitch architecture: uncaging
The supplied evidence indicates that LHCII has been examined in isolated native chlorophyll a/b-binding form and in recombinant form, with biochemical fractionation methods including sucrose gradient centrifugation and gel electrophoresis used to resolve associated complexes. Because LHCII is described as a chlorophyll-protein complex, practical use is likely tied to photosynthetic membrane context and pigment association, but the provided evidence does not specify construct architecture, host systems, or delivery methods.
The evidence is limited to a small number of studies focused on native photosynthetic context and biochemical characterization rather than generalizable tool engineering. Independent replication of the specific light-induced conformational exposure of the phosphorylation site and dimer-state behaviors is not established from the supplied evidence. No quantitative activation wavelengths, kinetics, dynamic range, or heterologous deployment data are provided.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper1992Journal of Biological Chemistry
Source 3primary paper1999Proceedings of the National Academy of Sciences
Ranked Claims
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
Approval Evidence
3 sources12 linked approval claimsfirst-pass slugs lhcii, light-harvesting-complex-ii
LHCII, the major photosynthetic antenna complex of plants
Source:
isolated native chlorophyll (chl) a/b light-harvesting complex II (LHCII), as well as recombinant LHCII
Source:
Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
Source:
functional propertysupports
One type of associated LHCII dimer is characterized by a high rate of chlorophyll excitation quenching.
the other formed by association of monomers into a distinctively different molecular organizational form, characterized by a high rate of chlorophyll excitation quenching
Source:
molecular state observationsupports
LHCII can appear in a dimeric state in addition to trimeric and monomeric states.
LHCII, the major photosynthetic antenna complex of plants, can appear not only in the trimeric or monomeric states but also as a dimer.
Source:
molecular state subtype observationsupports
Two types of LHCII dimers were observed: one produced by dissociation of one monomer from the trimeric structure and another produced by association of monomers into a distinct organizational form.
The results reveal the appearance of two types of LHCII dimers: one formed by the dissociation of one monomer from the trimeric structure and the other formed by association of monomers into a distinctively different molecular organizational form
Source:
physiological relevance hypothesissupports
High light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
The high light-induced LHCII dimerization is discussed as a potential element of the photoprotective response in plants.
Source:
mechanismsupports
A light-induced conformational change increases accessibility of the LHCII N-terminal domain, as evidenced by increased tryptic cleavage after light exposure.
The suggested light-induced conformational change exposing the N-terminal domain of LHCII to the kinase is evidenced also by an increase in its accessibility to tryptic cleavage after light exposure.
Source:
mechanismsupports
Illumination of the chlorophyll-protein substrate exposes the LHCII phosphorylation site to the thylakoid protein kinase.
we find that illumination of the chl-protein substrate exposes the phosphorylation site to the kinase
Source:
mechanismsupports
Light can regulate thylakoid protein phosphorylation not only through redox-linked kinase activation but also by altering the conformation of the chlorophyll-protein substrate.
These results demonstrate that light may regulate thylakoid protein phosphorylation not only via the signal transduction chain connecting redox reactions to the protein kinase activation, but also by affecting the conformation of the chl-protein substrate.
Source:
mechanismsupports
Light-induced exposure of the LHCII N-terminal domain to endogenous thylakoid protein kinase(s) and to tryptic cleavage also occurs in thylakoid membranes.
Light-induced exposure of the LHCII N-terminal domain to the endogenous protein kinase(s) and tryptic cleavage occurs also in thylakoid membranes.
Source:
negative resultsupports
Light does not activate phosphorylation of the LHCII apoprotein or of a pigment-reconstituted recombinant complex lacking the N-terminal domain containing the phosphothreonine site.
Light does not activate the phosphorylation of the LHCII apoprotein nor the recombinant pigment-reconstituted complex lacking the N-terminal domain that contains the phosphothreonine site.
Source:
preferencesupports
Light activates preferentially the trimeric form of LHCII, in parallel with chlorophyll fluorescence quenching.
Light activates preferentially the trimeric form of LHCII, and the process is paralleled by chl fluorescence quenching.
Source:
reversibilitysupports
The light-activated LHCII process and associated chlorophyll fluorescence quenching are slowly reversible in darkness.
Both phenomena are slowly reversible in darkness.
Source:
associationsupports
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
Source:
Comparisons
Source-backed strengths
Evidence supports multiple light-responsive molecular outputs in LHCII, including reversible conformational switching and formation of dimeric states in addition to monomeric and trimeric forms. Two dimer classes were observed, and one associated dimer type was characterized by a high rate of chlorophyll excitation quenching, indicating functionally distinct light-induced states. The literature also reports study of both isolated native chlorophyll a/b LHCII and recombinant LHCII.
Compared with AsLOV2
light-harvesting complex II and AsLOV2 address a similar problem space because they share recombination, signaling.
Shared frame: same top-level item type; shared target processes: recombination, signaling; shared mechanisms: conformational_uncaging; same primary input modality: light
Relative tradeoffs: appears more independently replicated; may reduce component-count burden.
Compared with Avena sativa phototropin-1 LOV2 domain
light-harvesting complex II and Avena sativa phototropin-1 LOV2 domain address a similar problem space because they share recombination, signaling.
Shared frame: same top-level item type; shared target processes: recombination, signaling; shared mechanisms: conformational_uncaging; same primary input modality: light
Strengths here: appears more independently replicated.
Compared with LHCII N-terminal domain
light-harvesting complex II and LHCII N-terminal domain address a similar problem space because they share recombination, signaling.
Shared frame: same top-level item type; shared target processes: recombination, signaling; shared mechanisms: conformational_uncaging, photocleavage; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
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