The archaeal sensory rhodopsin II/transducer complex:: a model for transmembrane signal transfer

被引:88
作者
Klare, JP
Gordeliy, VI
Labahn, J
Büldt, G
Steinhoff, HJ
Engelhard, M
机构
[1] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany
[2] Res Ctr Julich, Inst Biol Struct, D-52425 Julich, Germany
[3] Univ Osnabruck, Fachbereich Phys, D-49069 Osnabruck, Germany
关键词
phoborhodopsin; phototaxis; chemotaxis; signal transduction;
D O I
10.1016/S0014-5793(04)00193-0
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
Archaebacterial photoreceptors mediate phototaxis by regulating cell motility through two-component signalling cascades. Homologs of this sensory pathway occur in all three kingdoms of life, most notably in enteric bacteria in which the chemotaxis has been extensively studied. Recent structural and functional studies on the sensory rhodopsin II/transducer complex mediating the photophobic response of Natronomonas pharaonis have yielded new insights into the mechanisms of signal transfer across the membrane. Electron paramagnetic resonance data and the atomic resolution structure of the receptor molecule in complex with the transmembrane segment of its cognate transducer provided a model for signal transfer from the receptor to the cytoplasmic side of the transducer. This mechanism might also be relevant for eubacterial chemoreceptor signalling. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:219 / 224
页数:6
相关论文
共 49 条
[1]   METHYL-ACCEPTING TAXIS PROTEINS IN HALOBACTERIUM-HALOBIUM [J].
ALAM, M ;
LEBERT, M ;
OESTERHELT, D ;
HAZELBAUER, GL .
EMBO JOURNAL, 1989, 8 (02) :631-639
[2]   STRUCTURAL FEATURES OF METHYL-ACCEPTING TAXIS PROTEINS CONSERVED BETWEEN ARCHAEBACTERIA AND EUBACTERIA REVEALED BY ANTIGENIC CROSS-REACTION [J].
ALAM, M ;
HAZELBAUER, GL .
JOURNAL OF BACTERIOLOGY, 1991, 173 (18) :5837-5842
[3]   Bacterial tactic responses [J].
Armitage, JP .
ADVANCES IN MICROBIAL PHYSIOLOGY, VOL 41, 1999, 41 :229-289
[4]   Receptor clustering as a cellular mechanism to control sensitivity [J].
Bray, D ;
Levin, MD ;
Morton-Firth, CJ .
NATURE, 1998, 393 (6680) :85-88
[5]   Demonstration of 2:2 stoichiometry in the functional SRI-HtrI signaling complex in Halobacterium membranes by gene fusion analysis [J].
Chen, XP ;
Spudich, JL .
BIOCHEMISTRY, 2002, 41 (12) :3891-3896
[6]   The photophobic receptor from Natronobacterium pharaonis:: Temperature and pH dependencies of the photocycle of sensory rhodopsin II [J].
Chizhov, I ;
Schmies, G ;
Seidel, R ;
Sydor, JR ;
Lüttenberg, B ;
Engelhard, M .
BIOPHYSICAL JOURNAL, 1998, 75 (02) :999-1009
[7]  
Engelhard M, 2003, COMP SER PHOTOCHEM, V3, P1
[8]   The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes [J].
Falke, JJ ;
Bass, RB ;
Butler, SL ;
Chervitz, SA ;
Danielson, MA .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1997, 13 :457-512
[9]   Cooperativity between bacterial chemotaxis receptors [J].
Falke, JJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (10) :6530-6532
[10]   PROLINE RESIDUES UNDERGO STRUCTURAL-CHANGES DURING PROTON PUMPING IN BACTERIORHODOPSIN [J].
GERWERT, K ;
HESS, B ;
ENGELHARD, M .
FEBS LETTERS, 1990, 261 (02) :449-454