ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.
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ABSTRACT:
SUBMITTER: Haeusser DP
PROVIDER: S-EPMC2648377 | biostudies-literature | 2009 Mar
REPOSITORIES: biostudies-literature
Publications
ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.
Haeusser Daniel P DP Lee Amy H AH Weart Richard B RB Levin Petra Anne PA
Journal of bacteriology 20090109 6
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 chaper ...[more]
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