The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW.
AUTOR(ES)
Bourret, R B
RESUMO
The CheA kinase is a central protein in the signal transduction network that controls chemotaxis in Escherichia coli. CheA receives information from a transmembrane receptor (e.g., Tar) and CheW proteins and relays it to the CheB and CheY proteins. The biochemical activities of CheA proteins truncated at various distances from the carboxy terminus were examined. The carboxy-terminal portion of CheA regulates autophosphorylation in response to environmental signals transmitted through Tar and CheW. The central portion of CheA is required for autophosphorylation and is also presumably involved in dimer formation. The amino-terminal portion of CheA was previously shown to contain the site of autophosphorylation and to be able to transfer the phosphoryl group to CheB and CheY. These studies further delineate three functional domains of the CheA protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=204313Documentos Relacionados
- Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA.
- Both CheA and CheW are required for reconstitution of chemotactic signaling in Escherichia coli.
- CheA, CheW, and CheY are required for chemotaxis to oxygen and sugars of the phosphotransferase system in Escherichia coli.
- Phosphorylation of the RNA Polymerase II Carboxy-Terminal Domain by the Bur1 Cyclin-Dependent Kinase
- The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA