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Volume 143, Issue 10

Functional and genetic characterization of , which encodes a third methyl-accepting chemotaxis protein in Free

Abstract

A 3135 bp DNA segment downstream of the gene on the chromosome was cloned and its nucleotide sequence determined. An open reading frame capable of encoding a putative protein of 654 amino acids with a calculated molecular mass of 72.1 kDa was identified. The deduced amino acid sequence was similar to the McpA and McpB proteins of McpA and McpB encode different methyl-accepting chemotaxis proteins (MCPs). A mutant strain containing an antibiotic resistance DNA cassette inserted into the region containing the MCP-like reading frame suffered a complete loss of taxis to the amino acids cysteine, proline, threonine, glycine, serine, lysine, valine and arginine. The open reading frame was designated The wild-type and an mutant strain were analysed for their content of methylated proteins and it was found that encodes a methylated membrane protein that has previously been designated H3. These results show that encodes a third MCP in The transcription start site upstream of the gene was determined by primer extension analysis and it was found to be preceded by a potential promoter sequence that is recognized by the β form of RNA polymerase. The level of β-gaiactosidase expressed from a transcriptional fusion was increased threefold when cells entered the stationary phase. No β-gaiactosidase could be detected in a genetic background.

  • Received:
  • Accepted:
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  • Published Online:
Keyword(s): chemotaxis receptor protein , mcpC expression , mcpC gene sequence , methylation and σD-dependent expression
© Society for General Microbiology 1997
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1997-10-01
2024-04-18
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Functional and genetic characterization of mcpC, which encodes a third methyl-accepting chemotaxis protein in Bacillus subtilis
Microbiology 143, 3231 (1997); https://doi.org/10.1099/00221287-143-10-3231
/content/journal/micro/10.1099/00221287-143-10-3231
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