TAILIEUCHUNG - Báo cáo khoa học: Mycobacterium tuberculosis ClpC1 Characterization and role of the N-terminal domain in its function

Caseinolytic protein, ClpC is a general stress protein which belongs to the heat shock protein HSP100 family of molecular chaperones. Some of the Clp group proteins have been identified as having a role in the pathogene-sis of many bacteria. | ỊFEBS Journal Mycobacterium tuberculosis ClpC1 Characterization and role of the N-terminal domain in its function Narayani P. Kar Deepa Sikriwal Parthasarathi Rath Rakesh K. Choudhary and Janendra K. Batra Immunochemistry Laboratory National institute of Immunology New Delhi India Keywords chaperone heat shock proteins HSP100 protein aggregation protein refolding Correspondence J. K. Batra Immunochemistry Laboratory National institute of Immunology Aruna Asaf Ali Marg New Delhi 110067 India Fax 91 11 2674 2125 Tel 91 11 2670 3739 E-mail janendra@ These authors contributed equally to this work Received 31 July 2008 revised 7 October 2008 accepted 10 October 2008 doi Caseinolytic protein ClpC is a general stress protein which belongs to the heat shock protein HSP100 family of molecular chaperones. Some of the Clp group proteins have been identified as having a role in the pathogenesis of many bacteria. The Mycobacterium tuberculosis genome demonstrates the presence of a ClpC homolog ClpC1. M. tuberculosis ClpC1 is an 848-amino acid protein has two repeat sequences at its N-terminus and contains all the determinants to be classified as a member of the HSP100 family. In this study we overexpressed purified and functionally characterized M. tuberculosis ClpC1. Recombinant M. tuberculosis ClpC1 showed an inherent ATPase activity and prevented protein aggregation. Furthermore to investigate the contribution made by the N-terminal repeats of ClpC1 to its functional activity two deletion variants ClpC1D1 and ClpC1D2 lacking N-terminal repeat I and N-terminal repeat I along with the linker between N-terminal repeats I and II respectively were generated. Neither deletion affected the ATPase activity. However ClpC1D1 was structurally altered less stable and was unable to prevent protein aggregation. Compared with wild-type protein ClpC1D2 was more active in preventing protein aggregation and displayed higher ATPase activity at high pH

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