Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC

被引:4
|
作者
Miller, Erik J.
Meyer, Anne S.
Frydman, Judith
机构
[1] Stanford Univ, Dept Biol Sci, Stanford, CA 94305 USA
[2] Stanford Univ, Bio X Program, Stanford, CA 94305 USA
[3] Stanford Univ, Canc Biol Program, Stanford, CA 94305 USA
关键词
chaperonin; chaperone; TRiC; CCT; GroEL; protein folding; ring complex;
D O I
10.1110/ps.052001606
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1522 / 1526
页数:5
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