The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins

被引:187
作者
Aravind, L
Ponting, CP [1 ]
机构
[1] NIH, Natl Ctr Biotechnol Informat, Natl Lib Med, Bethesda, MD 20894 USA
[2] Texas A&M Univ, Dept Biol, College Stn, TX 77843 USA
关键词
histidine kinase; chemotaxis; PP2C-like phosphatase; adenylyl cyclase; PAS domain; regulator of receptor function; sequence analysis;
D O I
10.1016/S0378-1097(99)00197-4
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Mutations in the cytoplasmic linker regions of receptor histidine kinase and chemoreceptor proteins have been shown previously to significantly impair receptor functions. Here we demonstrate significant sequence similarities between these regions in numerous histidine kinases, methyl-accepting proteins, adenylyl cyclases and other prokaryotic signalling proteins. It is suggested that these 'HAMP domains' possess roles of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:111 / 116
页数:6
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