Novel bacterial rhodopsins from Haloarcula vallismortis.
New bacterial rhodopsins of the cruxrhodopsin (cR) tribe were identified in a type strain Haloarcula vallismortis. The genes encoding a bacteriorhodopsin-like ion pump (named cR-3), a halorhodopsin-like ion pump (chR-3) and a sensor rhodopsin (csR-3) were cloned and sequenced. Together with the data for vsRII (Seidel et al., Proc. Natl. Acad. Sci. USA 92, 3036-3040 (1995); cpR-3 in our notation), the primary structures of a set of four rhodopsins are now all known only in this species. They are separated by almost the same distances in homology, suggesting that they have derived from a single ancestral rhodopsin. The degree of conservation in the amino acid sequence of each helix showed that helices C and G are relatively well conserved in all rhodopsins, whereas helices DEF are conserved especially in sensor rhodopsin-I, possibly because these helices are needed for interaction with the transducer protein (Htr).
Kitajima
T
T
Department of Biology, School of Science, Nagoya University, Japan.
Hirayama
J
J
Ihara
K
K
Sugiyama
Y
Y
Kamo
N
N
Mukohata
Y
Y
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D001436:Bacteriorhodopsins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D001483:Base Sequence; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D017124:Conserved Sequence; D006217:Halobacterium / Q000737:chemistry*; D025602:Halorhodopsins; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017433:Protein Structure, Secondary; D012243:Rhodopsin / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment
D001426:Bacterial Proteins; D025602:Halorhodopsins; C099613:sensor rhodopsin csR-3, Haloarcula vallismortis; D001436:Bacteriorhodopsins; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D012243:Rhodopsin