What history tells us Ⅱ. The discovery of chaperone function

摘要

Twenty years ago, Hugh Pelham interpreted the effects observed after an overexpression of HSP70 in heat-stressed cells by the ability of this protein to disrupt the complexes of unfolded proteins that form under these conditions (Pelham 1984; Lewis and Pelham 1985). This was one of the important steps which led in less than five years to the emergence of the notion of chaperones. The history of the discovery of the chaperones was rich and tortuous. Chaperone function was the last of the main cellular functions to emerge from . . . nothing: both the central dogma of molecular biology and the experiments of Christian Anfinsen supported the hypothesis that the folding of proteins and their assembly into macromolecular complexes were spontaneous processes, requiring no assistance.