title: Sensory rhodopsin-I as a bidirectional switch: opposite conformational changes from the same photoisomerization.
abstract: The phototaxis receptor sensory rhodopsin I (SRI) exists in two protein conformations, each of which is converted to the other by light absorption by the protein's retinylidene chromophore. One conformer inhibits a histidine-kinase attached to its bound transducer HtrI and its formation induces attractant motility responses, whereas the other conformer activates the kinase and its formation induces repellent responses. We performed Fourier transform infrared spectroscopy with temperature, pH, and mutation-induced shifts in the conformer equilibrium, and found that both conformers when present in the unphotolyzed dark state contain an all-trans retinal configuration that is photoisomerized to 13-cis, i.e., the same photoisomerization causes the opposite conformational change in the photointerconvertible pair of conformers depending on which conformer is present in the dark. Therefore, switching between the protein global conformations that define the two conformers is independent of the direction of isomerization. Insights into this phenomenon are gained from analysis of the evolution of the receptor from light-driven proton pumps, which use similar conformers for transport. The versatility of the conformational changes of microbial rhodopsins, including conformer interexchangeability in the photocycle as shown here, is likely a significant factor in the evolution of the diverse functionality of this protein family.
authors.affiliation: Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas, USA.
authors.forename: Jun
authors.initials: J
authors.lastname: Sasaki
authors.forename: Hazuki
authors.initials: H
authors.lastname: Takahashi
authors.forename: Yuji
authors.initials: Y
authors.lastname: Furutani
authors.forename: Hideki
authors.initials: H
authors.lastname: Kandori
authors.forename: John L
authors.initials: JL
authors.lastname: Spudich
mesh_terms: D019843:Archaeal Proteins / Q000378:metabolism; D003624:Darkness; D019617:Halobacterium salinarum / Q000378:metabolism / Q000528:radiation effects; D007536:Isomerism; D008027:Light; D008565:Membrane Proteins / Q000378:metabolism; D009068:Movement / Q000528:radiation effects; D011487:Protein Conformation; D025603:Sensory Rhodopsins / Q000737:chemistry* / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
chemical_list: D019843:Archaeal Proteins; D008565:Membrane Proteins; D025603:Sensory Rhodopsins; C082504:htrI protein, Halobacterium salinarium