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Journal of Bacteriology, October 1998, p. 5123-5128, Vol. 180, No. 19
Department of Molecular and Cellular Biology,
Harvard University, Cambridge, Massachusetts 02138
Received 4 June 1998/Accepted 6 August 1998
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.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
CheZ Has No Effect on Flagellar Motors Activated
by CheY13DK106YW
*
Corresponding author. Mailing address: Department of
Molecular and Cellular Biology, Harvard University, Cambridge, MA
02138. Phone: (617) 495-0924. Fax: (617) 496-1114. E-mail:
hberg{at}biosun.harvard.edu.
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