YtvA from Bacillus subtilis is a LOV-domain photoswitch reported in this evidence set as a homodimeric light-responsive protein domain. It was highlighted in an optogenetics context because its relaxation half-life is longer than that of Avena sativa LOV2, suggesting potential utility as a light-controlled module.
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Mechanism Concept
homodimerization
A mechanism-level grouping derived from the current toolkit evidence. Current coverage includes 0 architectures and 3 components. Across those tools, the main enabled capabilities are signaling. Representative components include Rhodobacter sphaeroides light-oxygen-voltage domain, YtvA from Bacillus subtilis, and light-oxygen-voltage sensing (LOV) domain.
3 total items0 architectures3 components
Main enabled capabilities: signaling.
Components
3 of 3The light-oxygen-voltage sensing (LOV) domain is a blue light-responsive protein domain used in optogenetic constructs to confer light-dependent control over coupled signaling effectors. The supplied evidence specifically describes it as a blue light homodimerizing LOV domain.
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.