MHYT, a new integral membrane sensor domain

被引:32
作者
Galperin, MY [1 ]
Gaidenko, TA
Mulkidjanian, AY
Nakano, M
Price, CW
机构
[1] Natl Lib Med, Natl Ctr Biotechnol Informat, NIH, Bethesda, MD 20894 USA
[2] Univ Calif Davis, Dept Food Sci & Technol, Davis, CA 95616 USA
[3] Univ Osnabruck, Div Biophys, D-49069 Osnabruck, Germany
[4] Oregon Grad Inst Sci & Technol, Dept Biochem & Mol Biol, Beaverton, OR 97006 USA
关键词
genome analysis; protein domain; sequence conservation; anaerobic growth; signal transduction; metal binding;
D O I
10.1111/j.1574-6968.2001.tb10919.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
MHYT. a new conserved protein domain with a likely signaling function. is described. This domain consists of six transmembrane segments, three of which contain conserved methionine, histidine, and tyrosine residues that are projected to lie near the outer face of the cytoplasmic membrane. In Synechocystis sp. PCC6803, this domain forms the N-terminus of the sensor histidine kinase Slr2098. In Pseudomonas aeruginosa and several other organisms, the MHYT domain forms the N-terminal part of a three-domain protein together with previously described GGDEF and EAL domains. both of which have been associated with signal transduction due to their presence in likely signaling proteins. In Bacillus subtilis YkoW protein. an additional PAS domain is found between the MHYT and GGDEF domains. A ykoW null mutant of B. subtilis did not exhibit any growth alterations, consistent with a non-essential, signaling role of this protein. A model of the membrane topology of the MHYT domain indicates that its conserved residues could coordinate one or two copper ions. suggesting a role in sensing oxygen, CO, or NO. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:17 / 23
页数:7
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