This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fuhrer, D K Articles by Ordal, G W Search for Related Content PubMed PubMed Citation Articles by Fuhrer, D K Articles by Ordal, G W

 Previous Article  |  Next Article 

J Bacteriol. 1991 December; 173(23): 7443-7448

research-article

Bacillus subtilis CheN, a homolog of CheA, the central regulator of chemotaxis in Escherichia coli.

Department of Biochemistry, College of Medicine, University of Illinois, Urbana 61801.

ABSTRACT

The Bacillus subtilis cheN gene was isolated, sequenced, and expressed. It encodes a large negatively charged protein with a molecular weight of approximately 74,000. The predicted protein sequence has 33 to 34% identity with the Escherichia coli and Salmonella typhimurium CheA and Myxococcus xanthus FrzE sequences. These proteins are found to autophosphorylate and are members of the same histidine kinase signal modulating family. CheN has several conserved regions (including the histidine that is phosphorylated in CheA) that coincide with other autophosphorylated signal transducers. A null mutant is defective in attractant-induced methanol formation and shows no behavioral response to chemoeffectors. These results imply that in B. subtilis the mechanism of chemotaxis involves phosphoryl transfer similar to that in E. coli. However, the CheN null mutant mostly tumbles, whereas CheA mutants swim smoothly, and only in B. subtilis does excitation lead to methyl transfer and methanol formation. Thus, the overall mechanism of chemotaxis is different in the two organisms.

This article has been cited by other articles:

• Muff, T. J., Foster, R. M., Liu, P. J. Y., Ordal, G. W. (2007). CheX in the Three-Phosphatase System of Bacterial Chemotaxis. J. Bacteriol. 189: 7007-7013 [Abstract] [Full Text]  
• Dons, L., Eriksson, E., Jin, Y., Rottenberg, M. E., Kristensson, K., Larsen, C. N., Bresciani, J., Olsen, J. E. (2004). Role of Flagellin and the Two-Component CheA/CheY System of Listeria monocytogenes in Host Cell Invasion and Virulence. Infect. Immun. 72: 3237-3244 [Abstract] [Full Text]  
• Szurmant, H., Ordal, G. W. (2004). Diversity in Chemotaxis Mechanisms among the Bacteria and Archaea. Microbiol. Mol. Biol. Rev. 68: 301-319 [Abstract] [Full Text]  
• Szurmant, H., Muff, T. J., Ordal, G. W. (2004). Bacillus subtilis CheC and FliY Are Members of a Novel Class of CheY-P-hydrolyzing Proteins in the Chemotactic Signal Transduction Cascade. J. Biol. Chem. 279: 21787-21792 [Abstract] [Full Text]  
• Saulmon, M. M., Karatan, E., Ordal, G. W. (2004). Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis. Microbiology 150: 581-589 [Abstract] [Full Text]  
• Lux, R., Sim, J.-H., Tsai, J. P., Shi, W. (2002). Construction and Characterization of a cheA Mutant of Treponema denticola. J. Bacteriol. 184: 3130-3134 [Abstract] [Full Text]  
• Karatan, E., Saulmon, M. M., Bunn, M. W., Ordal, G. W. (2001). Phosphorylation of the Response Regulator CheV Is Required for Adaptation to Attractants during Bacillus subtilis Chemotaxis. J. Biol. Chem. 276: 43618-43626 [Abstract] [Full Text]  
• Kirby, J. R., Saulmon, M. M., Kristich, C. J., Ordal, G. W. (1999). CheY-dependent Methylation of the Asparagine Receptor, McpB, during Chemotaxis in Bacillus subtilis. J. Biol. Chem. 274: 11092-11100 [Abstract] [Full Text]  
• Zimmer, M. A., Tiu, J., Collins, M. A., Ordal, G. W. (2000). Selective Methylation Changes on the Bacillus subtilis Chemotaxis Receptor McpB Promote Adaptation. J. Biol. Chem. 275: 24264-24272 [Abstract] [Full Text]