title: Clp ATPases and their role in protein unfolding and degradation.
abstract: Although much has been learned about the structure and function of Clp chaperones and their role in proteolysis, the mechanism of protein unfolding catalyzed by Clp ATPases and the mechanism of translocation of the unfolded proteins from Clp ATPases to partner proteases remain unsolved puzzles. However, models in which mechanical force is used to destabilize the structure of the substrate in a processive and directional manner are probable. It also seems likely that when ClpA ATPases are associated with proteases, unfolding is coupled to extrusion of the unfolded protein into the proteolytic cavity. In summary, it is anticipated that the large family of Clp ATPases will accomplish their many important cellular functions by similar mechanisms and what has been learned by studying the prokaryotic members reviewed here will shed a great deal of light on all members of the family.
authors.affiliation: Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: J R
authors.initials: JR
authors.lastname: Hoskins
authors.forename: S
authors.initials: S
authors.lastname: Sharma
authors.forename: B K
authors.initials: BK
authors.lastname: Sathyanarayana
authors.forename: S
authors.initials: S
authors.lastname: Wickner
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D006868:Hydrolysis; D018832:Molecular Chaperones / Q000378:metabolism; D011489:Protein Denaturation; D013379:Substrate Specificity
chemical_list: D018832:Molecular Chaperones; D000251:Adenosine Triphosphatases