Novel bacterial rhodopsins from Haloarcula vallismortis

被引：18

作者：

Kitajima, T

Hirayama, J

Ihara, K

Sugiyama, Y

Kamo, N

Mukohata, Y

机构：

[1] NAGOYA UNIV,SCH SCI,DEPT BIOL,NAGOYA,AICHI 46401,JAPAN

[2] HOKKAIDO UNIV,FAC PHARMACEUT SCI,DEPT BIOPHYS CHEM,SAPPORO,HOKKAIDO 060,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 220卷 / 02期

关键词：

D O I：

10.1006/bbrc.1996.0407

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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). (C) 1996 Academic Press, Inc.

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页码：341 / 345

页数：5

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