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Nucleotide-dependent oligomerization of ClpB from Escherichia coli

Published online by Cambridge University Press:  01 September 1999

MICHAL ZOLKIEWSKI ,
MARTIN KESSEL ,
ANN GINSBURG  and
MICHAEL R. MAURIZI
MICHAL ZOLKIEWSKI
Affiliation:
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506
MARTIN KESSEL
Affiliation:
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892
ANN GINSBURG
Affiliation:
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892
MICHAEL R. MAURIZI
Affiliation:
Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892
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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 (ATPγS). In contrast, 2 mM ADP inhibits full oligomerization of ClpB. The apparent size of the ATP- or ATPγS-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.

Keywords

electron microscopyheat-shock proteinsnucleotide bindingprotein associationsedimentation equilibriumsedimentation velocity
Type
Research Article
Information
Protein Science , Volume 8 , Issue 9 , September 1999 , pp. 1899 - 1903
Copyright
© 1999 The Protein Society

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