Chaperonins keeping a lid on folding proteins
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Date
2001-09
Language
American English
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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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Kusmierczyk, A. R., & Martin, J. (2001). Chaperonins–keeping a lid on folding proteins. FEBS letters, 505(3), 343-347.
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Article