Published online by Cambridge University Press: 10 August 2009
Introduction
Like a Brian Rix farce, in which the characters' identities are continuously changing, the functions of the class of protein known as molecular chaperones has been unfolding continuously over the past decade resulting in substantial confusion. However, like such farces, we are confident that the dénouement will be a complete surprise and will provide a new world picture of the processes with which molecular chaperones are involved. This short chapter aims to introduce the reader to the rapidly changing world of molecular chaperones as an aid to the reading of the rest of the chapters in this volume.
Molecular chaperones are protein folders
Our story starts with a huff and a puff with the study of the response of the polytene chromosomes of Drosophila to various stressors. This revealed novel patterns of specific chromosomal puffs, in response to heat, and a variety of other environmental stresses, representing the transcription of selected genes [1, 2]. The behaviour of cells exposed to various stresses became known as the heat shock response or the cell stress response and we now appreciate the very large number of environmental factors to which cells will respond in this stereotypical manner. The ‘molecularisation’ of the cell stress response occurred in the late 1980s with the pioneering work of Ellis and colleagues [3], who introduced both the concept of protein chaperoning and the term molecular chaperone.
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