Source 1primary paper2012Plant and Cell Physiology
Toolkit/AUREO1 bZIP-LOV truncated construct
AUREO1 bZIP-LOV truncated construct
Also known as: ZL
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The AUREO1 bZIP-LOV truncated construct (ZL) is an N-terminally truncated aureochrome-1 derivative that retains the bZIP DNA-binding region and the LOV photosensory domain. It binds DNA in a sequence-specific manner and undergoes a blue-light-induced conformational response measurable as an approximately 5% increase in hydrodynamic radius without a detectable change in secondary structure.
Usefulness & Problems
Why this is useful
ZL is useful as a compact light-responsive DNA-binding module derived from aureochrome-1. It provides a system for studying or potentially exploiting blue-light control of a transcription factor-like protein state while preserving sequence-specific DNA binding.
Source:
Aureochrome-1 (AUREO1) is a blue light (BL) receptor that mediates the branching response in the stramenopile alga, Vaucheria frigida.
Problem solved
This construct addresses the need for a reduced aureochrome-1 variant that isolates the bZIP-LOV core while retaining light responsiveness and DNA-binding activity. The available evidence supports its use for dissecting how blue light alters the conformation of a DNA-binding photoreceptor protein.
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
ZL is an N-terminally truncated construct containing the bZIP and LOV regions of AUREO1. The evidence establishes blue-light responsiveness and sequence-specific DNA binding, but it does not provide construct boundaries, cofactor requirements, expression conditions, or delivery guidance.
Evidence is limited to a single cited study and focuses on biophysical characterization rather than engineered functional outputs. The supplied evidence does not demonstrate recombination control, in vivo switching performance, kinetics, reversibility, or independent replication.
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 source4 linked approval claimsfirst-pass slug aureo1-bzip-lov-truncated-construct
an N-terminal truncated construct containing bZIP and LOV (ZL)
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 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.
Source:
mechanistic modelsupports
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.
Source:
oligomeric statesupports
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.
Source:
Comparisons
Source-backed strengths
The construct preserves sequence-specific DNA binding, as reported for both full-length AUREO1 and ZL. Blue light produces a measurable conformational change in ZL, observed as an approximately 5% increase in hydrodynamic radius, while secondary structure remains unchanged.
Ranked Citations
- 1.