Chaperonins--keeping a lid on folding proteins.
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.
Kusmierczyk
A R
AR
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, P.O. Box G-J2, Providence, RI 02912, USA.
Martin
J
J
D018833:Chaperonins / Q000737:chemistry / Q000502:physiology*; D017510:Protein Folding; D013329:Structure-Activity Relationship
D018833:Chaperonins