Source 1primary paper2013Nucleic Acids Research
Toolkit/Rhodobacter sphaeroides light-oxygen-voltage domain
Rhodobacter sphaeroides light-oxygen-voltage domain
Also known as: RsLOV
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Rhodobacter sphaeroides light-oxygen-voltage domain (RsLOV) is a homodimeric LOV photosensory protein domain from Rhodobacter sphaeroides. Reported engineering results indicate that fusion of RsLOV to Cas9-derived effector variants can confer light sensitivity, and the same domain also imparted strong temperature sensitivity in that study.
Usefulness & Problems
Why this is useful
RsLOV is useful as a modular sensory domain for building externally controllable protein systems. The available evidence specifically supports its use in engineered Cas9-derived effectors to introduce regulation by light and temperature.
Problem solved
RsLOV helps address the problem of making Cas9-derived effector variants conditionally responsive to external stimuli. The cited study indicates that it enabled both light-switchable and strongly temperature-sensitive behavior in these engineered proteins.
Problem links
Need precise spatiotemporal control with light input
DerivedThe Rhodobacter sphaeroides light-oxygen-voltage domain (RsLOV) is a homodimeric LOV photosensory protein domain from R. sphaeroides. Reported engineering results indicate that this domain can be fused to Cas9-derived effector variants to confer light sensitivity, and in the same study it also imparted strong temperature sensitivity.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: 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: sensorswitch architecture: multi componentswitch architecture: recruitment
The available evidence supports implementation by domain fusion to Cas9-derived effector variants. RsLOV is described as a homodimeric LOV domain from Rhodobacter sphaeroides, but the provided material does not specify construct architecture, chromophore requirements, expression context, or illumination conditions.
The supplied evidence is limited to a brief description and two engineering claims from a single study. No quantitative performance data, illumination parameters, dynamic range, reversibility, kinetics, or validation across multiple targets or organisms are provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
RsLOV can confer light sensitivity onto Cas9-derived effector variants.
RsLOV can confer light sensitivity onto an unrelated effector
The same RsLOV domain can impart strong temperature sensitivity in addition to light sensitivity.
unexpectedly, the same LOV domain can also impart strong temperature sensitivity
Approval Evidence
1 source2 linked approval claimsfirst-pass slug rhodobacter-sphaeroides-light-oxygen-voltage-domain
the homodimeric Rhodobacter sphaeroides light-oxygen-voltage (LOV) domain (RsLOV)
Source:
engineering resultsupports
RsLOV can confer light sensitivity onto Cas9-derived effector variants.
RsLOV can confer light sensitivity onto an unrelated effector
Source:
engineering resultsupports
The same RsLOV domain can impart strong temperature sensitivity in addition to light sensitivity.
unexpectedly, the same LOV domain can also impart strong temperature sensitivity
Source:
Comparisons
Source-backed strengths
The evidence identifies RsLOV as a homodimeric LOV domain and reports successful transfer of stimulus responsiveness to Cas9-derived effector variants by fusion. A notable strength from the cited engineering result is that a single domain was associated with both light sensitivity and strong temperature sensitivity in the same study.
Source:
RsLOV can confer light sensitivity onto an unrelated effector
Source:
unexpectedly, the same LOV domain can also impart strong temperature sensitivity
Compared with light-oxygen-voltage sensing (LOV) domain
Rhodobacter sphaeroides light-oxygen-voltage domain and light-oxygen-voltage sensing (LOV) domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization, homodimerization; same primary input modality: light
Compared with optogenetic RGS2
Rhodobacter sphaeroides light-oxygen-voltage domain and optogenetic RGS2 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Compared with split-TurboID
Rhodobacter sphaeroides light-oxygen-voltage domain and split-TurboID address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.