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Heat-shock proteins as molecular chaperones

  • Chapter
EJB Reviews 1994

Part of the book series: EJB Reviews 1994 ((EJB REVIEWS,volume 1994))

Abstract

Functional proteins within cells are normally present in their native, completely folded form. However, vital processes of protein biogenesis such as protein synthesis and translocation of proteins into intracellular compartments require the protein to exist temporarily in an unfolded or partially folded conformation. As a consequence, regions buried when a polypeptide is in its native conformation become exposed and interact with other proteins causing protein aggregation which is deleterious to the cell. To prevent aggregation as proteins become unfolded, heat-shock proteins protect these interactive surfaces by binding to them and facilitating the folding of unfolded or nascent polypeptides. In other instances the binding of heat-shock proteins to interactive surfaces of completely folded proteins is a crucial part of their regulation. As heat shock and other stress conditions cause cellular proteins to become partially unfolded, the ability of heat-shock proteins to protect cells against the adverse effects of stress becomes a logical extension of their normal function as molecular chaperones.

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Abbreviations

ER:

endoplasmic reticulum

hsp:

heat-shock protein

hsc:

heat-shock cognate

SRP:

signal recognition particle

TCP1:

tailess-complex polypeptide 1

TRiC:

TCP1-containing ring complex.

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Becker, J., Craig, E.A. (1994). Heat-shock proteins as molecular chaperones. In: EJB Reviews 1994. EJB Reviews 1994, vol 1994. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79502-2_2

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