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- Title
Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone.
- Authors
Thibault, Guillaume; Tsitrin, Yulia; Davidson, Toni; Gribun, Anna; Houry, Walid A
- Abstract
The ClpXP ATPase-protease complex is a major component of the protein quality control machinery in the cell. A ClpX subunit consists of an N-terminal zinc binding domain (ZBD) and a C-terminal AAA+ domain. ClpX oligomerizes into a hexamer with the AAA+ domains forming the base of the hexamer and the ZBDs extending out of the base. Here, we report that ClpX switches between a capture and a feeding conformation. ZBDs in ClpX undergo large nucleotide-dependent block movement towards ClpP and into the AAA+ ring. This motion is modulated by the ClpX cofactor, SspB. Evidence for this movement was initially obtained by the surprising observation that an N-terminal extension on ClpX is clipped by bound ClpP in functional ClpXP complexes. Protease-protection, crosslinking, and light scattering experiments further support these findings.
- Publication
The EMBO journal, 2006, Vol 25, Issue 14, p3367
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1038/sj.emboj.7601223