In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.
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.
Sanna
M G
MG
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
Simon
M I
MI
D001426:Bacterial Proteins; D001665:Binding Sites; D002633:Chemotaxis; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D017353:Gene Deletion; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D016296:Mutagenesis; D010641:Phenotype
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli