The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW
Abstract
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.
Additional Information
Copyright © 1993 by the American Society for Microbiology. Received 21 October 1992/Accepted 12 January 1993 We thank Lisa Alex and Kathy Borkovich for the gift of materials; Eric Kofoid and Sandy Parkinson for providing the E. coli cheA sequence prior to publication; Lisa Alex, Kathy Borkovich, Andy Pakula, and Sandy Parkinson for helpful discussions; Germana Sanna for assistance with DNA sequencing; and Lisa Alex and Germana Sanna for comments on the manuscript. This work was supported by grant A119296 from the National Institutes of Health (to M.I.S.) and by National Research Service Award Fellowship A107798 (to R.B.B.).Files
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- Eprint ID
- 2706
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- CaltechAUTHORS:BOUjbact93
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2006-04-21Created from EPrint's datestamp field
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2019-10-02Created from EPrint's last_modified field