PMID:9405352
| Citation |
Liu, Y, Levit, M, Lurz, R, Surette, MG and Stock, JB (1997) Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J. 16:7231-40 |
|---|---|
| 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 approximately 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. |
| Links |
PubMed PMC1170323 Online version:10.1093/emboj/16.24.7231 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Bacterial Proteins/ultrastructure; Cell Membrane/physiology; Chemotaxis/physiology; Dimerization; Enzyme Activation; Escherichia coli/physiology; Escherichia coli Proteins; Kinetics; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Membrane Proteins/ultrastructure; Models, Molecular; Protein Kinases/metabolism; Salmonella typhimurium/physiology; Signal Transduction |
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