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

Jakob Müller, Stacey Schiel, George W. Ordal, Hans H. Saxild

Research output: Contribution to journalArticlepeer-review


A 3135 bp DNA segment downstream of the spl gene on the Bacillus subtilis 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 B. subtilis. 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 mcpC. The wild-type and an mcpC mutant strain were analysed for their content of methylated proteins and it was found that mcpC encodes a methylated membrane protein that has previously been designated H3. These results show that mcpC encodes a third MCP in B. subtilis. The transcription start site upstream of the mcpC gene was determined by primer extension analysis and it was found to be preceded by a potential promoter sequence that is recognised by the σ(D) form of RNA polymerase. The level of β-galactosidase expressed from a transcriptional mcpC-lacZ fusion was increased threefold when cells entered the stationary phase. No β-galactosidase could be detected in a sigD genetic background.

Original languageEnglish (US)
Pages (from-to)3231-3240
Number of pages10
Issue number10
StatePublished - Oct 1997
Externally publishedYes


  • Chemotaxis receptor protein
  • Methylation
  • mcpC expression
  • mcpC gene sequence
  • σ(D)-dependent expression

ASJC Scopus subject areas

  • Microbiology


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