Methyl-accepting chemotaxis protein III and transducer gene trg
نویسندگان
چکیده
منابع مشابه
Methyl group turnover on methyl-accepting chemotaxis proteins during chemotaxis by Bacillus subtilis.
The addition of attractant to Bacillus subtilis briefly exposed to radioactive methionine causes an increase of labeling of the methyl-accepting chemotaxis proteins. The addition of attractant to cells radiolabeled for longer times shows no change in the extent of methylation. Therefore, the increase in labeling for the briefly labeled cells is due to an increased turnover of methyl groups caus...
متن کاملGenetics of methyl-accepting chemotaxis proteins in Escherichia coli: cheD mutations affect the structure and function of the Tsr transducer.
The tsr gene specifies a methyl-accepting membrane protein involved in chemotaxis to serine and several repellent compounds. We have characterized a special class of tsr mutations designated cheD which alter the signaling properties of the Tsr transducer. Unlike tsr null mutants, cheD strains are generally nonchemotactic, dominant in complementation tests, and exhibit a pronounced counterclockw...
متن کاملPosttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli.
Methyl-accepting chemotaxis proteins (MCPs) of Escherichia coli undergo changes in methylation state in response to chemical stimuli. The addition of methyl groups to MCP is dependent on cheR function; their removal is dependent on cheB function. This MCP methylation system is instrumental in establishing the unstimulated swimming pattern of E. coli and in enabling the cell to carry out sensory...
متن کاملAn archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins.
Signal transduction in the archaeon Halobacterium salinarum is mediated by three distinct subfamilies of transducer proteins. Here we report the complete htrVIII gene sequence and present analysis of the encoded primary structure and its functional features. HtrVIII is a 642-amino-acid protein and belongs to halobacterial transducer subfamily B. At the N terminus, the protein contains six trans...
متن کاملPurification and Characterization of Bacillus subtilis Methyl - accepting Chemotaxis Protein Methyltransferase 11
A Bacillus subtilis methyltransferase capable of methylating membrane-bound methyl-accepting chemotaxis proteins (MCPs) of a chemotaxis mutant was purified to homogeneity. MCPs are normally unmethylated in this strain. Results of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicate that the enzyme is a 30,000 molecular weight monomer. The nzym...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1981
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.145.1.43-49.1981