Substrate Mutations That Bypass a Specific Cpn10 Chaperonin Requirement for Protein Folding

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Chaperonin-mediated protein folding: fate of substrate polypeptide.

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A Chaperonin Subunit with Unique Structures Is Essential for Folding of a Specific Substrate

Type I chaperonins are large, double-ring complexes present in bacteria (GroEL), mitochondria (Hsp60), and chloroplasts (Cpn60), which are involved in mediating the folding of newly synthesized, translocated, or stress-denatured proteins. In Escherichia coli, GroEL comprises 14 identical subunits and has been exquisitely optimized to fold its broad range of substrates. However, multiple Cpn60 s...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1998

ISSN: 0021-9258

DOI: 10.1074/jbc.273.51.34075