ArticleBiophysical journal2007
Different dark conformations function in color-sensitive photosignaling by the sensory rhodopsin I-HtrI complex.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Distance mapping in proteins using fluorescence spectroscopy: tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner.Biochemistry · 2014Article
- His166 is the Schiff base proton acceptor in attractant phototaxis receptor sensory rhodopsin I.Biochemistry · 2014Article
- Emerging approaches to probing ion channel structure and function.Neuroscience bulletin · 2012Review
- Opposite displacement of helix F in attractant and repellent signaling by sensory rhodopsin-Htr complexes.The Journal of biological chemistry · 2011Article
- Attractant and repellent signaling conformers of sensory rhodopsin-transducer complexes.Biochemistry · 2010Article
- A predictive computational model of the kinetic mechanism of stimulus-induced transducer methylation and feedback regulation through CheY in archaeal phototaxis and chemotaxis.BMC systems biology · 2010Article
- A Schiff base connectivity switch in sensory rhodopsin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Salinibacter sensory rhodopsin: sensory rhodopsin I-like protein from a eubacterium.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The haloarchaeal phototaxis receptor sensory rhodopsin I (SRI) in complex with its transducer HtrI delivers an attractant signal from excitation with an orange photon and a repellent signal from a second near-UV photon excitation. Using a proteoliposome system with purified SRI in complex with its transducer HtrI, we identified by site-directed fluorescence labeling a site (Ser(155)) on SRI that is conformationally active in signal relay to HtrI. Using site-directed spin labeling of Ser(155)Cys with a nitroxide side chain, we detected a change in conformation following one-photon excitation such that the spin probe exhibits a splitting of the outer hyperfine extrema (2A'(zz)) significantly smaller than that of the electron paramagnetic resonance spectrum in the dark state. The dark conformations of five mutant complexes that do not discriminate between orange and near-UV excitation show shifts to lower or higher 2A'(zz) values correlated with the alterations in their motility behavior to one- and two-photon stimuli. These data are interpreted in terms of a model in which the dark complex is populated by two conformers in the wild type, one that inhibits the CheA kinase (A) and the other that activates it (R), shifted in the dark by mutations and shifted in the wild-type SRI-HtrI complex in opposite directions by one-photon and two-photon reactions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.