SAGE-Hindawi Access to Research Journal of Amino Acids Volume 2011, Article ID 843206, 16 pages doi:10.4061/2011/843206 Review Article Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding M. Anaul Kabir,1 Wasim Uddin,1 Aswathy Narayanan,1 Praveen Kumar Reddy,1 M. Aman Jairajpuri,2 Fred Sherman,3 and Zulfiqar Ahmad4 1 Molecular Genetics Laboratory, School of Biotechnology, National Institute of Technology Calicut, Kerala 673601, India 2 Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India 3 Department of Biochemistry and Biophysics, University of Rochester Medical Center, NY 14642, USA 4 Department of Biology, Alabama A&M University, Normal, AL 35762, USA Correspondence should be addressed to M. Anaul Kabir,
[email protected] Received 15 February 2011; Accepted 5 April 2011 Academic Editor: Shandar Ahmad Copyright © 2011 M. Anaul Kabir et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Molecular chaperones are a class of proteins responsible for proper folding of a large number of polypeptides in both prokaryotic and eukaryotic cells. Newly synthesized polypeptides are prone to nonspecific interactions, and many of them make toxic aggregates in absence of chaperones. The eukaryotic chaperonin CCT is a large, multisubunit, cylindrical structure having two identical rings stacked back to back. Each ring is composed of eight different but similar subunits and each subunit has three distinct domains. CCT assists folding of actin, tubulin, and numerous other cellular proteins in an ATP-dependent manner.