CheZ has no effect on flagellar motors activated by CheY13DK106YW.
The behaviors of both cheZ-deleted and wild-type cells of Escherichia coli were found to be very sensitive to the level of expression of CheZ, a protein known to accelerate the dephosphorylation of the response regulator CheY-phosphate (CheY-P). However, cells induced to run and tumble by the unphosphorylated mutant protein CheY13DK106YW (CheY**) failed to respond to CheZ, even when CheZ was expressed at high levels. Therefore, CheZ neither affects the flagellar motors directly nor sequesters CheY**. In in vitro cross-linking studies, CheY** promoted trimerization of CheZ to the same extent as wild-type CheY but failed to induce the formation of complexes of higher molecular weight observed with CheY-P. Also, CheY** could be cross-linked to FliM, the motor receptor protein, nearly as well as CheY-P. Thus, to CheZ, CheY** looks like CheY, but to FliM, it looks like CheY-P.
Scharf
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BE
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Fahrner
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KA
Berg
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HC
D001426:Bacterial Proteins / Q000737:chemistry; D003432:Cross-Linking Reagents; D004926:Escherichia coli / Q000166:cytology*; D029968:Escherichia coli Proteins; D005407:Flagella / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D000072236:Methyl-Accepting Chemotaxis Proteins; D010766:Phosphorylation; D011487:Protein Conformation
D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607606:cheY protein, E coli; C066821:FliM protein, Bacteria