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Journal of Bacteriology, March 2009, p. 1986-1991, Vol. 191, No. 6
0021-9193/09/$08.00+0 doi:10.1128/JB.01606-07
Copyright © 2009, American Society for Microbiology. All Rights Reserved.
,
,
Amy H. Lee,
,¶
Richard B. Weart,# and
Petra Anne Levin*
Department of Biology, Washington University, Campus Box 1137, One Brookings Drive, St. Louis, Missouri 63130
Received 3 October 2007/ Accepted 29 December 2008
ClpX is a well-characterized bacterial chaperone that plays a role in many processes, including protein turnover and the remodeling of macromolecular complexes. All of these activities require ATP hydrolysis-dependent, ClpX-mediated protein unfolding. Here we used site-directed mutagenesis in combination with genetics and biochemistry to establish that ClpX inhibits assembly of the conserved division protein FtsZ through a noncanonical mechanism independent of its role as an ATP-dependent chaperone.
Published ahead of print on 9 January 2009.
Supplemental material for this article may be found at http://jb.asm.org/.
These authors contributed equally to this work.
Present address: Department of Biochemistry and Molecular Biology, Penn State University, University Park, PA 16801.
¶ Present address: Department of Cell and Systems Biology, University of Toronto, Toronto, ON, Canada M5S 3B2.
# Present address: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
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