MHYT, a new integral membrane sensor domain

DC FieldValueLanguage
dc.contributor.authorGalperin, MY
dc.contributor.authorGaidenko, TA
dc.contributor.authorMulkidjanian, AY
dc.contributor.authorNakano, M
dc.contributor.authorPrice, CW
dc.date.accessioned2021-12-23T16:21:03Z-
dc.date.available2021-12-23T16:21:03Z-
dc.date.issued2001
dc.identifier.issn03781097
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/13705-
dc.description.abstractMHYT. 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.
dc.description.sponsorshipNIGMS NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [GM 42077] Funding Source: Medline; NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM042077] Funding Source: NIH RePORTER
dc.language.isoen
dc.publisherELSEVIER SCIENCE BV
dc.relation.ispartofFEMS MICROBIOLOGY LETTERS
dc.subjectanaerobic growth
dc.subjectBACILLUS-SUBTILIS
dc.subjectCU-B
dc.subjectCYTOCHROME BO(3)
dc.subjectDATABASE
dc.subjectESCHERICHIA-COLI
dc.subjectgenome analysis
dc.subjectIDENTIFICATION
dc.subjectmetal binding
dc.subjectMicrobiology
dc.subjectPOLYMERASE
dc.subjectPROTEIN
dc.subjectprotein domain
dc.subjectRESPONSE REGULATOR
dc.subjectsequence conservation
dc.subjectsignal transduction
dc.subjectTRANSCRIPTION
dc.titleMHYT, a new integral membrane sensor domain
dc.typejournal article
dc.identifier.doi10.1111/j.1574-6968.2001.tb10919.x
dc.identifier.isiISI:000172471900003
dc.description.volume205
dc.description.issue1
dc.description.startpage17
dc.description.endpage23
dc.contributor.orcid0000-0002-2265-5572
dc.contributor.orcid0000-0001-5844-3064
dc.contributor.orcid0000-0002-0635-8535
dc.contributor.researcheridM-6900-2019
dc.contributor.researcheridB-5859-2013
dc.contributor.researcheridJ-8086-2013
dc.contributor.researcheridAAH-3608-2021
dc.publisher.placePO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
dcterms.isPartOf.abbreviationFEMS Microbiol. Lett.
dcterms.oaStatusBronze
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