PHOTOPHOSPHORYLATION ELEMENTS IN HALOBACTERIA - AN A-TYPE ATP SYNTHASE AND BACTERIAL RHODOPSINS

被引:10
作者
MUKOHATA, Y
SUGIYAMA, Y
IHARA, K
机构
[1] Department of Biology, Faculty of Science, Nagoya University, Nagoya
关键词
HALOBACTERIA; HALOPHILIC ARCHAEBACTERIA; PHOTOPHOSPHORYLATION; ATP SYNTHESIS; A-TYPE ATPASE; BACTERIAL RHODOPSINS; ARCHAERHODOPSIN; BACTERIORHODOPSIN;
D O I
10.1007/BF00762347
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Photophosphorylation in halobacteria is carried out by two rather simple elements: an A-type ATP synthase and light-driven ion-pumping bacterial rhodopsins. The unique features of halobacterial ATP synthase, mostly common to archaebacteria (A-type), and of new members of the bacteriorhodopsin family are introduced along with studies performed in the authors' laboratory. This is the story of how we found that the A-type ATP synthase is close to V-type ATPase but far from F-type ATPase, although all three ATPases are believed to have the same ancestor. Archaerhodopsins, the new members of the proton-pumping retinal proteins, were found in Australian halobacteria and have been used in a comparative study of bacterial rhodopsins.
引用
收藏
页码:547 / 553
页数:7
相关论文
共 58 条
[51]  
SCHOBERT B, 1982, J BIOL CHEM, V257, P306
[52]  
SCHOBERT B, 1989, J BIOL CHEM, V264, P12805
[53]  
SUGIYAMA Y, 1989, J BIOL CHEM, V264, P20859
[54]  
TAKAHASHI T, 1985, FEMS MICROBIOL LETT, V28, P161
[55]  
TSUDA M, 1982, BIOCHEM BIOPH RES CO, V108, P970
[56]   ARCHAERHODOPSIN-2, FROM HALOBACTERIUM SP AUS-2 FURTHER REVEALS ESSENTIAL AMINO-ACID-RESIDUES FOR LIGHT-DRIVEN PROTON PUMPS [J].
UEGAKI, K ;
SUGIYAMA, Y ;
MUKOHATA, Y .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1991, 286 (01) :107-110
[57]   PHYLOGENETIC STRUCTURE OF PROKARYOTIC DOMAIN - PRIMARY KINGDOMS [J].
WOESE, CR ;
FOX, GE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1977, 74 (11) :5088-5090
[58]  
YOKOYAMA K, 1990, J BIOL CHEM, V265, P21946