Source 1primary paper1999Proceedings of the National Academy of Sciences
Toolkit/LHCII N-terminal domain
LHCII N-terminal domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The LHCII N-terminal domain is the region of the light-harvesting complex II chlorophyll-protein substrate that contains the phosphothreonine site. In thylakoid studies, illumination induces a reversible conformational change that increases exposure of this N-terminal region, enabling access by endogenous thylakoid protein kinase(s) and increasing susceptibility to tryptic cleavage.
Usefulness & Problems
Why this is useful
This domain is useful as a native light-responsive substrate element for studying how illumination regulates thylakoid protein phosphorylation at the substrate level. It provides an experimentally observed example in which light changes protein accessibility rather than acting only through redox-linked kinase activation.
Problem solved
It helps address the problem of how light controls phosphorylation of LHCII by exposing the phosphothreonine-containing N-terminal region to thylakoid protein kinase(s). The cited work specifically links illumination to increased protease and kinase access through a conformational change in the chlorophyll-protein substrate.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational uncagingConformational Uncaginglight-induced substrate exposurePhotocleavageprotease accessibility changeTechniques
No technique tags yet.
Target processes
recombinationsignalingInput: Light
Implementation Constraints
The relevant functional feature is the LHCII N-terminal domain containing the phosphothreonine site within the chlorophyll-protein substrate. The reported assays were performed in thylakoid membranes and relied on illumination, endogenous thylakoid protein kinase activity, and tryptic cleavage as a readout of accessibility; no standalone construct design or delivery guidance is provided.
The evidence is limited to characterization of a native thylakoid substrate in the cited study and does not establish this domain as a portable engineered optogenetic module. No quantitative performance metrics, spectral parameters, or heterologous implementation data are provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
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
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 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.
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.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug lhcii-n-terminal-domain
the N-terminal domain that contains the phosphothreonine site
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
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:
Comparisons
Source-backed strengths
The reported response is supported by two concordant readouts: increased tryptic cleavage and increased exposure of the phosphorylation site to endogenous thylakoid protein kinase(s). The phenomenon was observed in thylakoid membranes, supporting relevance in a native membrane context.
Ranked Citations
- 1.