Abstract
Small stress proteins (also denoted small heat shock proteins: sHsp) are oligomeric phospho-polypeptides (Arrigo and Welch 1987; Arrigo et al. 1988; de Jong et al. 1993; Buchner et al. 1998) which increase the cell resistance to different types of stress, including heat shock and oxidative stress (reviewed in Arrigo and Landry 1994; Arrigo 1998, 2000; Arrigo and Préville 1999). In vitro, these proteins have been described as ATP-independent chaperones which counteract protein denaturation and help in the refolding of misfolded polypeptides (Jakob et al. 1993; Jakob and Buchner 1994; Ehrnsperger et al. 2000). Except for a role in maintaining cytoskeletal architecture, little information was available concerning the mode of action of these proteins in vivo. Recently, it has been proposed that large sHsp oligomers bind to misfolded polypeptides (Ehrnsperger et al. 1997; Lee et al. 1997) and present them to ATP-dependent protein chaperones (Hsp70, Hsp40, Hsp90 and co-chaperones) (see Haslbeck and Buchner, Chap. 3, this Vol.).
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Arrigo, AP., Paul, C., Ducasse, C., Sauvageot, O., Kretz-Remy, C. (2002). Small Stress Proteins: Modulation of Intracellular Redox State and Protection Against Oxidative Stress. In: Arrigo, AP., Müller, W.E.G. (eds) Small Stress Proteins. Progress in Molecular and Subcellular Biology, vol 28. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56348-5_9
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