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Sensory rhodopsin I: Receptor activation and signal relay

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Abstract

Recent progress is summarized on the mechanism of phototransduction by sensory rhodopsin I (SR-I), a phototaxis receptor inHalobacterium halobium. Two aspects are emphasized: (i)The coupling of retinal isomerization to protein conformational changes. Retinal analogs have been used to probe chromophore-apoprotein interactions during the receptor activation process. One of the most important results is the finding of a steric trigger deriving from the interaction of residues on the protein with a methyl group near the isomerizing bond of the retinal (at carbon 13). Recent work on molecular genetic methods to further probe structure/function includes the synthesis and expression of an SR-I apoprotein gene designed for residue replacements by cassette mutagenesis, and transformation of anH. halobium mutant lacking all retinylidene proteins known in this species to SR-I+ and bacteriorhodopsin (BR)+. (ii)The relay of the SR-I signal to a post-receptor component. A carboxylmethylated protein (“MPP-I”) associated with SR-I and found in theH. halobium membrane exhibits homology with the signaling domain of eubacterial chemotaxis transducers (e.g.,Escherichia coli Tar, Tsr, and Trg proteins), suggesting a model based on SR-I → MPP-I signal relay.

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Authors and Affiliations

  1. Department of Microbiology and Molecular Genetics, University of Texas Medical School, 77030, Houston, Texas

    John L. Spudich

  2. Department of Chemistry, University of California, 95035, Santa Cruz, California

    Roberto A. Bogomolni

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  1. John L. Spudich
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  2. Roberto A. Bogomolni
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Spudich, J.L., Bogomolni, R.A. Sensory rhodopsin I: Receptor activation and signal relay. J Bioenerg Biomembr 24, 193–200 (1992). https://doi.org/10.1007/BF00762677

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