Mande, S.C. and Mahajan, G. and Santosh , K.C.M. (2015) Multiple Chaperonins in Bacteria - Novel functions and Non-canonical behaviors. Cell Stress and Chaperones. pp. 1-15. ISSN CSAC-D-15-00022R2 (In Press)

Text 28. Dr. Mande (Cell Stress & Chaper - Author copy.pdf - Accepted Version Restricted to Registered users only until June 2016. Download (621Kb) | Request a copy

Abstract

Chaperonins are a class of molecular chaperones that assemble into large double ring architecture with each ring constituting 7-9 subunits and enclosing a cavity for substrate encapsulation. The well-studied E. coli chaperonin GroEL binds non-native substrates and encapsulates them in the cavity thereby sequestering the substrates from unfavorable conditions and allowing the substrates to fold. Using this mechanism, GroEL assists folding of about 10-15% of cellular proteins. Surprisingly, about 30% of the bacteria express multiple chaperonin genes. The presence of multiple chaperonins raises questions on whether they increase general chaperoning ability in the cell or have developed specific novel cellular roles. Although the latter view is widely supported, evidence for the former is beginning to appear. Some of these chaperonins can functionally replace GroEL in E. coli and are generally indispensable, while others are ineffective and likewise are dispensable. Additionally, moonlighting functions for several chaperonins have been demonstrated, indicating a functional diversity among the chaperonins. Furthermore, proteomics studies have identified diverse substrate pools for multiple chaperonins. We review the current perception on the multiple chaperonins and their physiological and functional specificities. Powered by

Item Type:	Article
Subjects:	Structural Biology
Depositing User:	Mr. Rameshwar Nema
Date Deposited:	12 May 2015 09:29
Last Modified:	15 May 2015 09:05
URI:	http://nccs.sciencecentral.in/id/eprint/174

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