The molecular chaperone concept.

R J Ellis; S M van der Vies; S M Hemmingsen

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PubMed · 2695089

The molecular chaperone concept.

R J Ellis·S M van der Vies·S M Hemmingsen

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Abstract

Molecular chaperones are a ubiquitous family of proteins whose proposed role is to mediate the folding and assembly of other proteins into oligomeric structures. The essential function of molecular chaperones is to prevent the formation of incorrect structures which may result from the transient exposure of charged or hydrophobic surfaces normally involved in interactions between or within polypeptide chains. Such transient exposure may occur during the synthesis of polypeptides, the unfolding and refolding that occurs during their transport across membranes, the association of polypeptides made in one subcellular compartment with those made in another, changes in protein-protein interactions during the normal functioning of a complex, and recovery from stresses such as heat shock. Three classes of molecular chaperone are discussed: the nucleoplasmins, the BiP group, and the chaperonins.

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Bacterial Proteins Carrier Proteins Endoplasmic Reticulum Chaperone BiP Escherichia coli Heat-Shock Proteins Mitochondria Molecular Chaperones Nuclear Proteins Nucleoplasmins Phosphoproteins Plant Proteins Protein Conformation Protein Denaturation Proteins Journal Article

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R J Ellis, S M van der Vies, S M Hemmingsen. 1989. The molecular chaperone concept.. https://pubmed.ncbi.nlm.nih.gov/2695089/

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