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Trends Biochem Sci. 1998 Feb;23(2):68-73.

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms.

Author information

1
Cornell Graduate School of Medical Sciences, New York, NY 10021, USA.

Abstract

Recent findings suggest that a combination of chaperonin-assisted and unassisted mechanisms operate in protein folding in the cytosol. While nascent chain-binding chaperones, such as Hsp70, could have a general role in maintaining the folding competence of translating polypeptide chains, the contribution of the cylindrical chaperonin complexes to overall folding is limited to a subset of aggregation-sensitive polypeptides. The majority of bacterial proteins are relatively small and they are synthesized rapidly and folded independently of the chaperonin GroEL in a posttranslational manner. Eukaryotes have a proportionally larger number of multi-domain proteins than bacteria. The individual domains of these proteins can be folded cotranslationally and sequentially. The use of this mechanism explains how large proteins fold independently of a chaperonin and could have been crucial in the evolution of a wide array of modular polypeptides in eukaryotes.

PMID:
9538692
DOI:
10.1016/s0968-0004(97)01171-7
[Indexed for MEDLINE]

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