Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis

George D. Glekas, Matthew J. Plutz, Hanna E. Walukiewicz, George M. Allen, Christopher V. Rao, George W. Ordal

Research output: Contribution to journalArticle

Abstract

Chemotaxis by Bacillus subtilis requires the CheD protein for proper function. In a cheD mutant when McpB was the sole chemoreceptor in B. subtilis, chemotaxis to asparagine was quite good. When McpC was the sole chemoreceptor in a cheD mutant, chemotaxis to proline was very poor. The reason for the difference between the chemoreceptors is because CheD deamidates Q609 in McpC and does not deamidate McpB. When mcpC-Q609E is expressed as the sole chemoreceptor in a cheD background, chemotaxis is almost fully restored. Concomitantly, in vitro McpC activates the CheA kinase poorly, whereas McpC-Q609E activates it much more. Moreover, CheD, which activates chemoreceptors, binds better to McpC-Q609E compared with unmodified McpC. Using hydroxyl radical susceptibility in the presence or absence of CheD, the most likely sites of CheD binding were the modification sites where CheD, CheB and CheR carry out their catalytic activities. Thus, CheD appears to have two separate roles in B. subtilis chemotaxis - to bind to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system and to deamidate selected residues to activate the chemoreceptors and enable them to mediate amino acid chemotaxis.

Original languageEnglish (US)
Pages (from-to)743-756
Number of pages14
JournalMolecular Microbiology
Volume86
Issue number3
DOIs
StatePublished - Nov 1 2012

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Chemotaxis
Bacillus subtilis
Asparagine
Proline
Hydroxyl Radical
Phosphotransferases
Binding Sites
Amino Acids

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis. / Glekas, George D.; Plutz, Matthew J.; Walukiewicz, Hanna E.; Allen, George M.; Rao, Christopher V.; Ordal, George W.

In: Molecular Microbiology, Vol. 86, No. 3, 01.11.2012, p. 743-756.

Research output: Contribution to journalArticle

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