Chaperonins – keeping a lid on folding proteins

FEBS Letters

Martin, Jörg¹  Kusmierczyk, Andrew R¹ 

[1] Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, P.O. Box G-J2, Providence, RI 02912, USA

关键词: Protein folding;    Chaperonin;    GroEL;    Chaperonin containing TCP-1;    Thermosome;    GroES;    CCT;    chaperonin containing TCP-1;   

DOI  :  10.1016/S0014-5793(01)02838-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two classes of chaperonins are known in all groups of organisms to participate in the folding of newly synthesized proteins. Whereas bacterial type I chaperonins use a reversibly binding cofactor to temporarily sequester folding substrate proteins within the cylindrical chaperonin cavity, type II chaperonins in archaea and the eukaryotic cytosol appear to have evolved a built-in lid for this purpose. Not entirely surprisingly, this has consequences for the folding modes of the two types of chaperonins.

【 授权许可】

Unknown