ArticleThe Journal of biological chemistry2008
Salinibacter sensory rhodopsin: sensory rhodopsin I-like protein from a eubacterium.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Cryo-EM structure of the SRI-HtrI complex reveals the cytoplasmic coupling in an archaeal phototaxis system.Nature communications · 2026Article
- Expression of microbial rhodopsins inSTAR protocols · 2022Article
- Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization.Scientific reports · 2021Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Applicability of Styrene-Maleic Acid Copolymer for Two Microbial Rhodopsins, RxR and HsSRI.Biophysical journal · 2020Article
- Photoreaction pathways and photointermediates of retinal-binding photoreceptor proteins as revealed by in situ photoirradiation solid-state NMR spectroscopy.Biophysical reviews · 2019Review
- Retinal Configuration of ppR Intermediates Revealed by Photoirradiation Solid-State NMR and DFT.Biophysical journal · 2018Article
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Light-controlled motility in prokaryotes and the problem of directional light perception.FEMS microbiology reviews · 2017Review
- Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K.Biochemistry · 2017Article
- A phylogenetically distinctive and extremely heat stable light-driven proton pump from the eubacterium Rubrobacter xylanophilus DSM 9941Scientific reports · 2017Article
- Enlightening the photoactive site of channelrhodopsin-2 by DNP-enhanced solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Microbial rhodopsins: wide distribution, rich diversity and great potential.Biophysics and physicobiology · 2015Review
- His166 is the Schiff base proton acceptor in attractant phototaxis receptor sensory rhodopsin I.Biochemistry · 2014Article
- Chimeric proton-pumping rhodopsins containing the cytoplasmic loop of bovine rhodopsin.PloS one · 2014Article
- Thermal and spectroscopic characterization of a proton pumping rhodopsin from an extreme thermophile.The Journal of biological chemistry · 2013Article
- A blue-shifted light-driven proton pump for neural silencing.The Journal of biological chemistry · 2013Article
- Chimeric microbial rhodopsins containing the third cytoplasmic loop of bovine rhodopsin.Biophysical journal · 2011Article
- Spectral tuning in sensory rhodopsin I from Salinibacter ruber.The Journal of biological chemistry · 2011Article
- A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halobacterium salinarum sensory rhodopsin I (HsSRI), a dual receptor regulating both negative and positive phototaxis in haloarchaea, transmits light signals through changes in protein-protein interactions with its transducer, halobacterial transducer protein I (HtrI). Haloarchaea also have another sensor pigment, sensory rhodopsin II (SRII), which functions as a receptor regulating negative phototaxis. Compared with HsSRI, the signal relay mechanism of SRII is well characterized because SRII from Natronomonus pharaonis (NpSRII) is much more stable than HsSRI and HsSRII, especially in dilute salt solutions and is much more resistant to detergents. Two genes encoding SRI homologs were identified from the genome sequence of the eubacterium Salinibacter ruber. Those sequences are distantly related to HsSRI ( approximately 40% identity) and contain most of the amino acid residues identified as necessary for its function. To determine whether those genes encode functional protein(s), we cloned and expressed them in Escherichia coli. One of them (SrSRI) was expressed well as a recombinant protein having all-trans retinal as a chromophore. UV-Vis, low-temperature UV-Vis, pH-titration, and flash photolysis experiments revealed that the photochemical properties of SrSRI are similar to those of HsSRI. In addition to the expression system, the high stability of SrSRI makes it possible to prepare large amounts of protein and enables studies of mutant proteins that will allow new approaches to investigate the photosignaling process of SRI-HtrI.
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