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Chaperone Function of sHsps

  • Chapter
Small Stress Proteins

Part of the book series: Progress in Molecular and Subcellular Biology ((PMSB,volume 28))

Abstract

Small heat shock proteins (sHsps) are a widespread but diverse class of proteins. In contrast to other families of Hsps, they contain certain conserved sequence motifs only in the C-terminal part of the protein, the so called occrystallin domain. These are low molecular mass proteins (15—42kDa) which form oligomeric structures ranging from 9 to 50 subunits. sHsps display a chaperone function in vitro. In addition, it has been suggested that they are involved in the inhibition of apoptosis, organization of the cytoskeleton and contribute to the optical properties of the eye lens in the case of α-crystallin. How these different functions can be explained by a common mechanism is unclear at the present state of investigations. However, as most of the observed phenomena involve non-native protein, the repeatedly reported chaperone properties of sHsps seem to be of key importance for understanding their function.

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Authors and Affiliations

  1. Institut für Organische Chemie und Biochemie, Technische Universität München, 85747, Garching, Germany

    Johannes Buchner

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  1. Martin Haslbeck
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  2. Johannes Buchner
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  1. Laboratoire Stress Oxydant Chaperons et Apoptose Centre de Génétique Moléculaire et Cellulaire CNRS UMR-5534, Université Claude Bernard Lyon-I, 43, Bd. du 11 Novembre, 69622, Villeurbanne, France

    André-Patrick Arrigo

  2. Institut für Physiologische Chemie Abteilung für Angewandte Molekularbiologie, Johannes Gutenberg-Universität, Duesbergweg 6, 55099, Mainz, Germany

    W. E. G. Müller

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Haslbeck, M., Buchner, J. (2002). Chaperone Function of sHsps. 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_3

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