Journal
PROTEIN SCIENCE
Volume 15, Issue 6, Pages 1522-1526Publisher
WILEY
DOI: 10.1110/ps.052001606
Keywords
chaperonin; chaperone; TRiC; CCT; GroEL; protein folding; ring complex
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM074074] Funding Source: NIH RePORTER
- NCI NIH HHS [CA09302, T32 CA009302] Funding Source: Medline
- NIGMS NIH HHS [GM74074, R01 GM074074] Funding Source: Medline
Ask authors/readers for more resources
The eukaryotic cytosolic chaperonin TRiC (TCP-1 Ring Complex), also known as CCT (Cytosolic Chaperonin containing TCP-1), is a hetero-oligomeric complex consisting of two back-to-back rings of eight different subunits each. The general architecture of the complex has been determined, but the arrangement of the subunits within the complex remains an open question. By assuming that the subunits have a defined arrangement within each ring, we constructed a simple model of TRiC that analyzes the possible arrangements of individual subunits in the complex. By applying the model to existing data, we find that there are only four subunit arrangements consistent with previous observations. Our analysis provides a framework for the interpretation and design of experiments to elucidate the quaternary structure of TRiC/CCT. This in turn will aid in the understanding of substrate binding and allosteric properties of this chaperonin.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available