Molecular mechanism of photosignaling by archaeal sensory rhodopsins.
Two sensory rhodopsins (SRI and SRII) mediate color-sensitive phototaxis responses in halobacteria. These seven-helix receptor proteins, structurally and functionally similar to animal visual pigments, couple retinal photoisomerization to receptor activation and are complexed with membrane-embedded transducer proteins (HtrI and HtrII) that modulate a cytoplasmic phosphorylation cascade controlling the flagellar motor. The Htr proteins resemble the chemotaxis transducers from Escherichia coli. The SR-Htr signaling complexes allow studies of the biophysical chemistry of signal generation and relay, from the photobiophysics of initial excitation of the receptors to the final output at the level of the flagellar motor switch, revealing fundamental principles of sensory transduction and more broadly the nature of dynamic interactions between membrane proteins. We review here recent advances that have led to new insights into the molecular mechanism of signaling by these membrane complexes.
Hoff
W D
WD
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston 77030-1501, USA.
Jung
K H
KH
Spudich
J L
JL
D000595:Amino Acid Sequence; D019843:Archaeal Proteins; D001436:Bacteriorhodopsins / Q000502:physiology*; D002338:Carotenoids; D006217:Halobacterium / Q000502:physiology*; D025602:Halorhodopsins; D008969:Molecular Sequence Data; D025603:Sensory Rhodopsins; D015398:Signal Transduction / Q000502:physiology*
D019843:Archaeal Proteins; D025602:Halorhodopsins; C061497:SRI protein, Halobacterium; D025603:Sensory Rhodopsins; C061508:sensory rhodopsin II protein, archaeal; D002338:Carotenoids; D001436:Bacteriorhodopsins