Source 1primary paper2018PLoS ONE
Toolkit/Vivid
Vivid
Also known as: VVD
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Vivid (VVD) is a blue-light-sensing light-oxygen-voltage (LOV) protein from the filamentous fungus Neurospora crassa. Upon illumination, its flavin cofactor forms a photoadduct that creates a stable light state, while VVD also exhibits light-dependent dimer-associated aggregation behavior and photosensitized self-oxidation.
Usefulness & Problems
Why this is useful
VVD is useful as a light-responsive protein domain because blue light drives a defined LOV photoadduct state with altered protein stability and kinetics. The reported light-dependent control of dimer formation and aggregation indicates potential utility in engineering light-regulated protein behavior through domain fusion, although the supplied evidence is centered on VVD biophysics rather than application performance.
Source:
Here we report that VVD presents alternative outcomes to light exposure that result in protein self-oxidation... Using optical absorbance and mass spectrometry we show that purified VVD develops amorphous aggregates with the presence of oxidized residues located at the cofactor binding pocket. Light exposure increases oxidative levels in VVD
Source:
Furthermore, photoadduct formation confers VVD stability against chemical denaturation.
Source:
In accordance, repeated BL illumination suppresses VVD aggregation altogether.
Source:
These results indicate that VVD acts alternatively as a photosensitizer, inducing self-oxidative damage and subsequent aggregation.
Problem solved
VVD helps address the problem of coupling blue-light input to reversible changes in protein state and assembly. The evidence specifically supports light-induced kinetic control over VVD stability, self-oxidation, and aggregation timing through photoadduct formation and decay.
Problem links
Need conditional recombination or state switching
DerivedVivid (VVD) is a blue-light-sensing light-oxygen-voltage (LOV) protein from the filamentous fungus Neurospora crassa. Upon illumination, VVD forms a light-induced photoadduct and undergoes dimer-associated state changes, while also exhibiting photosensitizing self-oxidation and light-dependent aggregation behavior.
Need precise spatiotemporal control with light input
DerivedVivid (VVD) is a blue-light-sensing light-oxygen-voltage (LOV) protein from the filamentous fungus Neurospora crassa. Upon illumination, VVD forms a light-induced photoadduct and undergoes dimer-associated state changes, while also exhibiting photosensitizing self-oxidation and light-dependent aggregation behavior.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
dimer formationdimer formationHeterodimerizationHeterodimerizationlight-dependent kinetic control of aggregationlight-dependent kinetic control of aggregationlight-induced photoadduct formationlight-induced photoadduct formationphotosensitizationphotosensitizationsinglet oxygen generationsinglet oxygen generationTechniques
No technique tags yet.
Target processes
recombinationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
VVD is a LOV-domain photoreceptor from Neurospora crassa and therefore depends on a flavin chromophore for blue-light sensing. The only engineering-related evidence supplied is domain fusion as a technique category; no specific fusion partners, expression systems, illumination parameters, or delivery methods are described in the provided material.
The evidence provided comes from a single study focused on oxidative damage, stability, and aggregation, rather than broad tool deployment in engineered systems. Photosensitized self-oxidation and aggregation are potential liabilities, and no quantitative performance data, construct architectures, or validation in recombination control are supplied here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Light exposure causes self-oxidation in VVD.
Here we report that VVD presents alternative outcomes to light exposure that result in protein self-oxidation... Using optical absorbance and mass spectrometry we show that purified VVD develops amorphous aggregates with the presence of oxidized residues located at the cofactor binding pocket. Light exposure increases oxidative levels in VVD
Photoadduct formation confers VVD stability against chemical denaturation.
Furthermore, photoadduct formation confers VVD stability against chemical denaturation.
Repeated blue-light illumination suppresses VVD aggregation altogether.
In accordance, repeated BL illumination suppresses VVD aggregation altogether.
VVD can act as a photosensitizer that induces self-oxidative damage and subsequent aggregation.
These results indicate that VVD acts alternatively as a photosensitizer, inducing self-oxidative damage and subsequent aggregation.
Aggregation in VVD proceeds through light-dependent kinetic control and dimer formation.
Analysis of the aggregation kinetics and testing of stabilizers against aggregation reveal that aggregation in VVD proceeds through light-dependent kinetic control and dimer formation.
Light-induced adduct formation establishes a stable state in VVD that delays aggregation until photoadduct decay occurs.
We show that light-induced adduct formation establishes a stable state, delaying protein aggregation until photoadduct decay occurs.
The flavin in VVD produces singlet oxygen upon light exposure.
specific probe analysis identifies singlet oxygen production by the flavin
Approval Evidence
1 source7 linked approval claimsfirst-pass slug vivid
The light-oxygen-voltage (LOV) protein Vivid (VVD) from the filamentous fungus Neurospora crassa is a classic BL photoreceptor.
Source:
functional propertysupports
Light exposure causes self-oxidation in VVD.
Here we report that VVD presents alternative outcomes to light exposure that result in protein self-oxidation... Using optical absorbance and mass spectrometry we show that purified VVD develops amorphous aggregates with the presence of oxidized residues located at the cofactor binding pocket. Light exposure increases oxidative levels in VVD
Source:
functional propertysupports
Photoadduct formation confers VVD stability against chemical denaturation.
Furthermore, photoadduct formation confers VVD stability against chemical denaturation.
Source:
functional propertysupports
Repeated blue-light illumination suppresses VVD aggregation altogether.
In accordance, repeated BL illumination suppresses VVD aggregation altogether.
Source:
functional propertysupports
VVD can act as a photosensitizer that induces self-oxidative damage and subsequent aggregation.
These results indicate that VVD acts alternatively as a photosensitizer, inducing self-oxidative damage and subsequent aggregation.
Source:
mechanismsupports
Aggregation in VVD proceeds through light-dependent kinetic control and dimer formation.
Analysis of the aggregation kinetics and testing of stabilizers against aggregation reveal that aggregation in VVD proceeds through light-dependent kinetic control and dimer formation.
Source:
mechanismsupports
Light-induced adduct formation establishes a stable state in VVD that delays aggregation until photoadduct decay occurs.
We show that light-induced adduct formation establishes a stable state, delaying protein aggregation until photoadduct decay occurs.
Source:
mechanismsupports
The flavin in VVD produces singlet oxygen upon light exposure.
specific probe analysis identifies singlet oxygen production by the flavin
Source:
Comparisons
Source-backed strengths
The supplied literature shows that photoadduct formation confers stability against chemical denaturation and establishes a stable state that delays aggregation until photoadduct decay. VVD also displays a strong light-responsive flavin chemistry, including singlet oxygen generation and light-dependent dimer-associated aggregation, and repeated blue-light illumination was reported to suppress aggregation altogether.
Compared with nMag/pMag photodimerization system
Vivid and nMag/pMag photodimerization system address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: looks easier to implement in practice.
Compared with optogenetic RGS2
Vivid and optogenetic RGS2 address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light
Compared with SspB
Vivid and SspB address a similar problem space because they share recombination.
Shared frame: same top-level item type; shared target processes: recombination; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.
Derived from 7 linked claims. Example evidence: Here we report that VVD presents alternative outcomes to light exposure that result in protein self-oxidation... Using optical absorbance and mass spectrometry we show that purified VVD develops amorphous aggregates with the presence of oxidized residues located at the cofactor binding pocket. Light exposure increases oxidative levels in VVD