Synonyms
Heat shock proteins (Hsp); Molecular chaperones (note: not all molecular chaperones are stress proteins); Polypeptide chain-binding proteins; Stress proteins (note: not all stress proteins are molecular chaperones, heat shock is one form of cellular stress, and glucose deprivation is another one)
Definition
Chaperones bind to exposed hydrophobic surfaces of polypeptide substrates and, through either ATP-dependent or ATP-independent mechanism, facilitate the folding/assembly, intracellular transport, and activity of polypeptides.
Basic Mechanisms
Molecular Chaperones
The term molecular chaperone was coined by Ron A. Laskey and coworkers in 1978 to describe the properties of the nuclear protein nucleoplasmin in assisting the in vitro assembly of nucleosomes from isolated histones and DNA (Laskey et al. 1978). Laskey introduced the term molecular chaperoneto describe the function of nucleoplasmin because of the analogy with the human chaperone. The role of a human chaperone was...
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References
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Zimmermann, R. (2021). Chaperones. In: Offermanns, S., Rosenthal, W. (eds) Encyclopedia of Molecular Pharmacology. Springer, Cham. https://doi.org/10.1007/978-3-030-57401-7_238
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DOI: https://doi.org/10.1007/978-3-030-57401-7_238
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