Journal
TRENDS IN MICROBIOLOGY
Volume 14, Issue 11, Pages 480-487Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2006.09.005
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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 Ca2+ channel activity. More than two decades since the discovery of the first sensory rhodopsins in the archaeon Halobacterium satinarum, 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.
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