ClpX Inhibits FtsZ Assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity

Daniel P. Haeusser, Amy H. Lee, Richard B. Weart, Petra Anne Levin

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1986-1991
Number of pages6
JournalJournal of bacteriology
Volume191
Issue number6
DOIs
StatePublished - Mar 2009

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