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 language | English |
---|---|
Pages (from-to) | 1986-1991 |
Number of pages | 6 |
Journal | Journal of bacteriology |
Volume | 191 |
Issue number | 6 |
DOIs | |
State | Published - Mar 2009 |