ClpX Inhibits FtsZ Assembly in a Manner That Does Not Require Its ATP Hydrolysis-Dependent Chaperone Activity

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 combin...

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Bibliographic Details
Main Authors: Haeusser, Daniel P., Lee, Amy H., Weart, Richard B., Levin, Petra Anne
Format: Artigo
Language:Inglês
Published: American Society for Microbiology (ASM) 2009
Subjects:
Genetics and Molecular Biology
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2648377/
https://ncbi.nlm.nih.gov/pubmed/19136590
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.01606-07
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