The multitalented microbial sensory rhodopsins.
Sensory rhodopsins are photoactive, membrane-embedded seven-transmembrane helix receptors that use retinal as a chromophore. They are widespread in the microbial world in each of the three domains of life: Archaea, Bacteria and Eukarya. A striking characteristic of these photoreceptors is their different modes of signaling in different organisms, including interaction with other membrane proteins, interaction with cytoplasmic transducers and light-controlled Ca(2+) channel activity. More than two decades since the discovery of the first sensory rhodopsins in the archaeon Halobacterium salinarum, genome projects have revealed a widespread presence of homologous photosensors. New work on cyanobacteria, algae, fungi and marine proteobacteria is revealing how evolution has modified the common design of these proteins to produce a remarkably rich diversity in their signaling biochemistry.
Spudich
John L
JL
Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School at Houston, Houston, TX 77030, USA. john.L.spudich@uth.tmc.edu
D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D025604:Rhodopsins, Microbial / Q000737:chemistry / Q000502:physiology*; D025603:Sensory Rhodopsins / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
D025604:Rhodopsins, Microbial; D025603:Sensory Rhodopsins