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Small Heat Shock Proteins in Physiological and Stress-Related Processes

  • Chapter
Cell Stress Proteins

Part of the book series: Protein Reviews ((PRON,volume 7))

Abstract

The small heat shock proteins (sHsps) family comprises several members found in prokaryotes and eukaryotes with important variations in the number of members between species (e.g., ,10 in mammals, ,20 in plants) (Kappe et al., 2002; Fu et al., 2006). Their common feature is a central α-crystallin domain. The core structure of the α-crystallin domain, rather than its amino acid sequence, is conserved between species. This ,90 amino acid domain presents a well-preserved double β-sheet sandwich structure, which is surrounded by N- and C-terminal domains whose length and sequence can vary extensively between and within species giving rise to proteins ranging from 11 to 42 kilodaltons (kDa). These extensions have been suggested to confer functional specificities to the different sHsps. Another property of sHsps is their propensity to form large oligomers, which are in dynamic equilibrium with smaller subunits (dimers, trimers, or tetramers depending on the sHsp). From X-ray and electron microscopic data, these particles have a diameter of 10–18 nm with a hollow core. The number of subunits can vary from 12 (Mycobacterium tuberculosis) to 24 (Methanocaldo coccus jannaschii and yeast). The quaternary structure is quite variable with polydisperse complexes in the range of 400 to over 800 kDa (see Sun and MacRae, 2005a; Haslbeck et al., 2005 for recent detailed reviews on the structure of sHsps).

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Orejuela, D., Bergeron, A., Morrow, G., Tanguay, R.M. (2007). Small Heat Shock Proteins in Physiological and Stress-Related Processes. In: Calderwood, S.K. (eds) Cell Stress Proteins. Protein Reviews, vol 7. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39717-7_7

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