Chaperonins--keeping a lid on folding proteins
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Updated: Oct 4, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
1Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, P.O. Box G-J2, Providence, RI 02912, USA.
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.
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