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Functional and Structural Characterization of Helicobacter pylori ClpX: A Molecular Chaperone of Hsp100 Family

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ClpX is a general stress protein which belongs to the heat shock protein, Clp/Hsp100 family of molecular chaperones. ClpX, in association with ClpP degrades proteins in an ATP dependent manner. Some members of the Clp family have been shown to be involved in the pathogenesis of many bacteria. The Helicobacter pylori genome demonstrates the presence of ClpX along with ClpA, ClpB and ClpP, the other members of the caseinolytic protease family. H. pylori ClpX is a 386 amino acid long protein. In this study, we have over-expressed H. pylori ClpX in E. coli, purified the recombinant protein to homogeneity and functionally characterized it. The recombinant H. pylori ClpX showed an inherent ATPase activity and prevented the heat induced aggregation of a model protein in vitro. The chaperonic activity of H. pylori ClpX was dependent on ATP hydrolysis and involved hydrophobic interaction with the substrate protein. Biophysical studies reveal the secondary structure tolerance of ClpX at various temperatures and in the presence of guanidine hydrochloride. The study demonstrates that H. pylori ClpX manifests chaperonic activity in the absence of any adaptor protein.
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Keywords: ATPase; DNA transposition; caseinolytic protease; chaperone; heat shock proteins; prion-like factors; prokaryotes; protease; protein folding; proteins

Document Type: Research Article

Publication date: December 1, 2012

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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