PMID:10493591

Citation	Zolkiewski, M, Kessel, M, Ginsburg, A and Maurizi, MR (1999) Nucleotide-dependent oligomerization of ClpB from Escherichia coli. Protein Sci. 8:1899-903
Abstract	Self-association of ClpB (a mixture of 95- and 80-kDa subunits) has been studied with gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. Monomeric ClpB predominates at low protein concentration (0.07 mg/mL), while an oligomeric form is highly populated at >4 mg/mL. The oligomer formation is enhanced in the presence of 2 mM ATP or adenosine 5'-O-thiotriphosphate (ATPgammaS). In contrast, 2 mM ADP inhibits full oligomerization of ClpB. The apparent size of the ATP- or ATPgammaS-induced oligomer, as determined by gel filtration, sedimentation velocity and electron microscopy image averaging, and the molecular weight, as determined by sedimentation equilibrium, are consistent with those of a ClpB hexamer. These results indicate that the oligomerization reactions of ClpB are similar to those of other Hsp100 proteins.
Links	PubMed PMC2144395 Online version:10.1110/ps.8.9.1899
Keywords	Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/chemistry; Affinity Labels; Chromatography, Gel; Dimerization; Escherichia coli/chemistry; Escherichia coli Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Heat-Shock Proteins/ultrastructure; Ultracentrifugation
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