ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Haeusser DP,Lee AH,Weart RB,Levin PA

doi

10.1128/JB.01606-07

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

1986-91

issue

6

eissn

0021-9193

issn

1098-5530

pii

JB.01606-07

journal_volume

191

pub_type

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