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