TY - JOUR
T1 - MHYT, a new integral membrane sensor domain
AU - Galperin, Michael Y.
AU - Gaidenko, Tatiana A.
AU - Mulkidjanian, Armen Y.
AU - Nakano, Michiko
AU - Price, Chester W.
N1 - Funding Information:
This research was supported in part by Public Health Service grant GM42077 (C.W.P.) and by a Deutsche Forschungsgemeinschaft travel grant (A.Y.M.). Analysis of unfinished genome sequences has been made possible by generous submission to the public databases of preliminary sequence data by the Sanger Centre ( B. pertussis , Bordetella parapertussis , B. bronchiseptica , B. pseudomallei , S. typhi ), the Institute for Genomic Research ( B. mallei , P. putida , P. syringae ), and the Washington University Genome Sequencing Center ( S. enterica , S. paratyphi ).
PY - 2001/11/27
Y1 - 2001/11/27
N2 - 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.
AB - 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.
KW - Anaerobic growth
KW - Genome analysis
KW - Metal binding
KW - Protein domain
KW - Sequence conservation
KW - Signal transduction
UR - http://www.scopus.com/inward/record.url?scp=0035960720&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035960720&partnerID=8YFLogxK
U2 - 10.1016/S0378-1097(01)00424-4
DO - 10.1016/S0378-1097(01)00424-4
M3 - Article
C2 - 11728710
AN - SCOPUS:0035960720
SN - 0378-1097
VL - 205
SP - 17
EP - 23
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
IS - 1
ER -