Sanna, M. Germana and Simon, Melvin I. (1996) In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants. Journal of Bacteriology, 178 (21). pp. 6275-6280. ISSN 0021-9193 http://resolver.caltech.edu/CaltechAUTHORS:SANjbact96
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Bacterial chemotaxis results from the ability of flagellated bacteria to control the frequency of switching between smooth-swimming and tumbling episodes in response to changes in concentration of extracellular substances. High levels of phosphorylated CheY protein are the intracellular signal for inducing the tumbling mode of swimming. The CheZ protein has been shown to control the level of phosphorylated CheY by regulating its rate of dephosphorylation. To identify functional domains in the CheZ protein, we made mutants by random mutagenesis of the cheZ gene and constructed a series of deletions. The map position and the in vivo and in vitro activity of the resulting gain- or loss-of-function mutant proteins define separate functional domains of the CheZ protein.
|Additional Information:||Copyright © 1996, American Society for Microbiology Received 29 April 1996/Accepted 26 August 1996 This work was supported by grant AI19296 from the National Institutes of Health. We thank Lisa Alex and Ron Swanson for critically reading the manuscript and Steve Marsh, Rick Colayco, and Barbara Perry for DNA sequencing. ADDENDUM IN PROOF: A recent paper (Y. Blat and M. Eisenbach, Biochemistry 35:5679–5683, 1996) also describes CheZ domain structure.|
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|Deposited On:||24 Apr 2006|
|Last Modified:||26 Dec 2012 08:50|
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