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Department of Microbiology, Technical University of Denmark, Bldg 301, DK-2800 Lyngby, Denmark
Department of Biochemistry, University of Illinois, 190 Medical Sciences Bldg, 506 S. Mathews Ave, Urbana, IL 61801-3618, USA
1 Author for correspondence: Hans H. Saxild. Tel: +45 45 25 24 95. Fax: +45 45 88 26 60. e-mail: hhs@im.dtu.dk
ABSTRACT
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 recognized by the βD form of RNA polymerase. The level of β-gaiactosidase expressed from a transcriptional mcpC-lacZ fusion was increased threefold when cells entered the stationary phase. No β-gaiactosidase could be detected in a sigD genetic background.
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