Signal Transfer in Haloarchaeal Sensory Rhodopsin– Transducer Complexes

Authors

  • Jun Sasaki,

    1. Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX
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  • John L. Spudich

    Corresponding author
    1. Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, TX
    2. Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX
      *Corresponding author email: john.l.spudich@uth.tmc.edu (John L. Spudich)
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  • This invited paper is part of the Symposium-in-Print: Photoreceptors and Signal Transduction.

*Corresponding author email: john.l.spudich@uth.tmc.edu (John L. Spudich)

Abstract

Membrane-inserted complexes consisting of two photochemically reactive sensory rhodopsin (SR) subunits flanking a homodimer of a transducing protein subunit (Htr) are used by halophilic archaea for sensing light gradients to modulate their swimming behavior (phototaxis). The SR–Htr complexes extend into the cytoplasm where the Htr subunits bind a his-kinase that controls a phosphorylation system that regulates the flagellar motors. This review focuses on current progress primarily on the mechanism of signal relay within the SRII–HtrII complexes from Natronomonas pharaonis and Halobacterium salinarum. The recent elucidation of a photoactive site steric trigger crucial for signal relay, advances in understanding the role of proton transfer from the chromophore to the protein in SRII activation, and the localization of signal relay to the membrane-embedded portion of the SRII–HtrII interface, are beginning to produce a clear picture of the signal transfer process. The SR–Htr complexes offer unprecedented opportunities to resolve first examples of the chemistry of signal relay between membrane proteins at the atomic level, which would provide a major contribution to the general understanding of dynamic interactions between integral membrane proteins.

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