Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis

Yi Liu, Mikhail Levit, Rudi Lurz, Michael G. Surette, Jeffry B. Stock

Research output: Contribution to journalArticle

117 Scopus citations

Abstract

Chemotaxis responses of Escherichia coli and Salmonella are mediated by type I membrane receptors with N-terminal extracytoplasmic sensing domains connected by transmembrane helices to C-terminal signaling domains in the cytoplasm. Receptor signaling involves regulation of an associated protein kinase, CheA. Here we show that kinase activation by a soluble signaling domain construct involves the formation of a large complex, with ~14 receptor signaling domains per CheA dimer. Electron microscopic examination of these active complexes indicates a well defined bundle composed of numerous receptor filaments. Our findings suggest a mechanism for transmembrane signaling whereby stimulus-induced changes in lateral packing interactions within an array of receptor-sensing domains at the cell surface perturb an equilibrium between active and inactive receptor-kinase complexes within the cytoplasm.

Original languageEnglish (US)
Pages (from-to)7231-7240
Number of pages10
JournalEMBO Journal
Volume16
Issue number24
DOIs
StatePublished - Dec 15 1997

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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