Source 1primary paper2014ACS Synthetic Biology
Toolkit/YF1
YF1
Also known as: engineered light-oxygen-voltage (LOV) histidine kinase YF1, engineered LOV photoreceptor YF1
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
YF1 is an engineered light-oxygen-voltage (LOV) histidine kinase that acts as a blue-light-regulated signaling switch. Available evidence indicates that blue-light input is transmitted through structural transitions in the photosensor and linker regions that control its signaling state.
Usefulness & Problems
Why this is useful
YF1 is useful as a model and engineered photoreceptor for controlling signaling with blue light while enabling mechanistic dissection of signal transmission in LOV-histidine kinase systems. The cited studies specifically use YF1 to map light-dependent structural changes and to test how mutations affect light regulation.
Problem solved
YF1 helps address the problem of converting blue-light reception into a regulated histidine kinase signaling output in an engineered receptor. It also provides a tractable system for resolving how structural transitions in LOV photoreceptors and associated linkers encode signaling state changes.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
Structural CharacterizationTarget processes
signalingInput: Light
Implementation Constraints
YF1 has been studied using site-directed mutagenesis, site-directed spin labelling, and ELDOR spectroscopy to monitor blue-light-induced structural transitions. The provided evidence identifies it as an engineered LOV histidine kinase, but does not specify construct architecture, host expression system, chromophore handling, or delivery constraints.
The supplied evidence is focused on mechanistic structural studies and mutational perturbation rather than broad application benchmarks or quantitative performance metrics. Independent replication, organism-specific deployment details, and comparative validation across diverse biological contexts are not established by the provided sources.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2017Scientific Reports
Ranked Claims
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Mutations near the flavin chromophore in LOV photoreceptors modulate response kinetics and effective light responsiveness.
For the blue-light-sensitive light-oxygen-voltage (LOV) photoreceptors, mutations near the flavin chromophore modulate response kinetics and the effective light responsiveness.
Carefully chosen mutations can adjust the light-response function of photoreceptors for diverse applications.
Carefully chosen mutations provide a powerful means to adjust the light-response function of photoreceptors as demanded for diverse applications.
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
Approval Evidence
2 sources8 linked approval claimsfirst-pass slug yf1
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
Source:
we introduced these mutations into the engineered LOV photoreceptor YF1 and determined their impact on light regulation
Source:
comparative mechanismsupports
A photoreceptor variant with an inverted signal response has a drastically altered dimer interface but shows linker structural transitions similar to those in YF1 under light stimulation.
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
Source:
generalizationsupports
The study provides mechanistic insight into signal trajectories of LOV photoreceptors and histidine kinases that can inform molecular simulations and engineering of novel receptors.
Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.
Source:
mechanistic insightsupports
In the engineered LOV histidine kinase YF1, blue-light reception involves structural transitions that can be charted by ELDOR spectroscopy and site-directed spin labelling.
Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1
Source:
structural mechanismsupports
Structural modelling based on ELDOR-derived pair-wise distance constraints indicates that light induces rotation and splaying apart of the two LOV photosensors in dimeric YF1.
Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor.
Source:
structural mechanismsupports
The molecular strain generated by light-induced photosensor rearrangement likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units.
Source:
biophysical correlationsupports
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain benign mutations on chromophore environment and response kinetics in YF1 and the Avena sativa phototropin 1 LOV2 domain.
Electron paramagnetic resonance and absorption spectroscopy identified correlated effects for certain of the latter mutations on chromophore environment and response kinetics in YF1 and the LOV2 domain from Avena sativa phototropin 1.
Source:
mutation effectsupports
In YF1, mutations I39V, R63K, and N94A severely impaired receptor dynamic range.
While several mutations severely impaired the dynamic range of the receptor (e.g., I39V, R63K, and N94A)
Source:
mutation effectsupports
In YF1, mutations V28T, N37C, and L82I were benign with little effect on regulation.
residue substitutions in a second group were benign with little effect on regulation (e.g., V28T, N37C, and L82I)
Source:
Comparisons
Source-backed strengths
The available evidence supports a defined blue-light-responsive mechanism in which structural transitions can be directly charted by electron-electron double resonance (ELDOR) spectroscopy combined with site-directed spin labelling. YF1 was also amenable to mutational analysis of light regulation, indicating that its signaling behavior can be probed experimentally at the structural and functional levels.
Source:
ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1.
Source:
For the blue-light-sensitive light-oxygen-voltage (LOV) photoreceptors, mutations near the flavin chromophore modulate response kinetics and the effective light responsiveness.
Source:
Carefully chosen mutations provide a powerful means to adjust the light-response function of photoreceptors as demanded for diverse applications.
Ranked Citations
- 1.
- 2.