Source 1primary paper2012Plant and Cell Physiology
Toolkit/full-length AUREO1 construct
full-length AUREO1 construct
Also known as: FL
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The full-length AUREO1 construct is a blue-light-responsive transcription factor from Vaucheria frigida that contains an N-terminal bZIP domain and a C-terminal LOV domain. In the reported study, the full-length protein binds DNA in a sequence-specific manner and undergoes an approximately 5% blue-light-induced increase in hydrodynamic radius.
Usefulness & Problems
Why this is useful
This construct is useful as a naturally occurring light-responsive DNA-binding protein that couples blue-light sensing to transcription-factor architecture. It provides a basis for studying and potentially exploiting optical control of sequence-specific DNA association and light-dependent conformational responses.
Source:
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Problem solved
It addresses the problem of linking a defined light input to a transcription-factor scaffold with sequence-specific DNA binding. The cited work specifically supports its use for investigating how blue light alters the conformation of a DNA-binding photoreceptor.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
recombinationInput: Light
Implementation Constraints
The reported construct is the full-length AUREO1 protein from Vaucheria frigida, comprising an N-terminal bZIP domain and a C-terminal LOV domain. The evidence supports blue-light responsiveness and sequence-specific DNA binding, but does not provide practical details on expression system, chromophore handling, delivery strategy, or construct optimization.
The supplied evidence is limited to one study and does not report performance in heterologous systems, dynamic range of transcriptional output, or recombination control. The available data describe hydrodynamic and DNA-binding properties, but do not directly demonstrate light-regulated gene expression by the full-length construct in an engineered context.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
AUREO1 contains an N-terminal bZIP domain and a C-terminal LOV domain.
AUREO1 harbors a basic leucine zipper (bZIP) domain at the N-terminus and a light-oxygen-voltage-sensing (LOV) domain within the C-terminal region
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Aureochrome-1 is a blue-light receptor that mediates the branching response in Vaucheria frigida.
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces an approximately 5% increase in hydrodynamic radius of the ZL construct without changing its secondary structure.
BL induced an approximately 5% increase in the R(H) of ZL, although its secondary structure was unchanged.
hydrodynamic radius change 5 %
Blue light induces a shift in the LOV-only construct from alpha-helical to beta-sheet secondary structure without altering hydrodynamic radius.
BL appeared to induce a shift of the α-helical structure of the LOV domain to a β-sheet structure, but did not alter the hydrodynamic radius (R(H)) of this domain.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Blue-light-induced changes in the LOV domain may cause conformational changes in the bZIP and/or linker region of dimeric ZL.
These results support a schema where BL-induced changes in the LOV domain may cause conformational changes in the bZIP and/or the linker of a dimeric ZL molecule.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
The ZL construct forms a dimer, possibly through disulfide linkages in the bZIP and linker regions.
ZL formed a dimer possibly through disulfide linkages in the bZIP and the linker region between bZIP and LOV.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug full-length-aureo1-construct
a full-length AUREO1 (FL)
Source:
dna bindingsupports
Full-length AUREO1 and the ZL construct bind DNA in a sequence-specific manner.
FL and ZL bound to DNA in a sequence-specific manner.
Source:
light induced hydrodynamic changesupports
Blue light induces an approximately 5% increase in hydrodynamic radius of the full-length AUREO1 construct.
Since a 5% increase of the R(H) was also observed with the FL construct
Source:
mechanistic modelsupports
Formation of the full-length AUREO1 dimer may facilitate DNA binding.
formation of the FL dimer may facilitate DNA binding.
Source:
Comparisons
Source-backed strengths
The construct combines a bZIP DNA-binding module with a LOV photosensory domain in a single full-length protein. Experimental evidence shows sequence-specific DNA binding and a measurable blue-light-induced increase in hydrodynamic radius, indicating a light-responsive conformational change in the intact factor.
Ranked Citations
- 1.