chaperonin; chaperone

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Introduction

Molecular chaperones or chaperonins constitute distinct families of proteins that are ubiquitous & highly conserved from bacteria to humans. They appear to bind non-native conformations of most, if not all proteins, thereby preventing their aggregation & subsequent inactivation. Chaperonins not only protect newly synthesized proteins during transport & folding, but serve to maintain cells in a healthy state during exposure to a multitude of stress conditions. Chaperonins are expressed constitutively, but their synthesis is enhanced during stress conditions. In mitochondrial protein biogenesis, chaperonins act as unfoldases, pulling devices & foldases.

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References

  1. Martinus RD et al Role of chaperones in the biogenesis and maintenance of the mitochondrion. FASEB J. 1995 Mar;9(5):371-8. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7896006