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Kumar, C.M.S. and Mande, S.C. (2017) Functional diversity in mycobacterial chaperonins: the generalists and the specialists. In: Prokaryotic Chaperonins. Heat Shock Proteins VOL. 15, 15 . Springer, pp. 67-80.

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Chaperonins are a class of molecular chaperones that form cylindrical assemblies and for sequestering the non-native protein and thereby assisting their folding. Genomic annotation studies have identified multiple copies of chaperonin genes in about 30% of the bacteria. Mycobacterium tuberculosis was the first organism where two copies were observed, and similarly other mycobacteria bear two and rarely three copies. Owing to the pathogenic lifestyle, the chaperonins of mycobacteria have been demonstrated to be secretory and possess antigenic properties. Furthermore, biochemical and structural studies have demonstrated that these chaperonins are unusual. One of the chaperonins that exists in operonic arrangement with the co-chaperonin gene has been shown to be required in several pathogenic stages of the bacteria. The other copy that exists independently is essential and thus might be functioning as a general chaperone. Several groups have worked to unravel the functional diversity of these mysterious molecules employing structural, immunochemical, cell-biological, computational and genetic tools. We review the current understanding on the mycobacterial chaperonins and the new paradigms that have arisen.

Item Type: Book Section
Subjects: Structural Biology
Depositing User: Mr. Rameshwar Nema
Date Deposited: 17 Dec 2018 11:52
Last Modified: 17 Dec 2018 11:52
URI: http://nccs.sciencecentral.in/id/eprint/575

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