MHYT, a new integral membrane sensor domain

Autor(en): Galperin, MY
Gaidenko, TA
Mulkidjanian, AY
Nakano, M
Price, CW
Stichwörter: anaerobic growth; BACILLUS-SUBTILIS; CU-B; CYTOCHROME BO(3); DATABASE; ESCHERICHIA-COLI; genome analysis; IDENTIFICATION; metal binding; Microbiology; POLYMERASE; PROTEIN; protein domain; RESPONSE REGULATOR; sequence conservation; signal transduction; TRANSCRIPTION
Erscheinungsdatum: 2001
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEMS MICROBIOLOGY LETTERS
Volumen: 205
Ausgabe: 1
Startseite: 17
Seitenende: 23
Zusammenfassung: 
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.
ISSN: 03781097
DOI: 10.1111/j.1574-6968.2001.tb10919.x

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