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Molecular Chaperones pp 69–98Cite as

Small Heat-Shock Proteins: Paramedics of the Cell

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Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 328))

Abstract

The small heat-shock proteins (sHSPs) comprise a family of molecular chaperones which are widespread but poorly understood. Despite considerable effort, comparatively few high-resolution structures have been determined for the sHSPs, a likely consequence of their tendency to populate ensembles of inter-converting conformational and oligomeric states at equilibrium. This dynamic structure appears to underpin the sHSPs’ ability to bind and sequester target proteins rapidly, and renders them the first line of defence against protein aggregation during disease and cellular stress. Here we describe recent studies on the sHSPs, with a particular focus on those which have provided insight into the structure and dynamics of these proteins. The combined literature reveals a picture of a remarkable family of molecular chaperones whose thermodynamic and kinetic properties are exquisitely balanced to allow functional regulation by subtle changes in cellular conditions.

Gillian R. Hilton, Hadi Lioe and Florian Stengel contributed equally to this work.

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Abbreviations

Af :

Archaeoglobus fulgidus

At :

Arabidopsis thaliana

Bt :

Bos taurus (cow)

Dr :

Danio rerio (zebrafish)

E. coli :

Escherichia coli

EM:

Electron microscopy

EPR:

Electron paramagnetic resonance spectroscopy

Hs :

Homo sapiens (human)

IM:

Ion mobility

Mj :

Methanocaldococcus jannaschii

MS:

Mass spectrometry

Mt :

Mycobacterium tuberculosis

nES:

Nanoelectrospray

NMR:

Nuclear magnetic resonance spectroscopy

Ps :

Pisum sativum (pea)

Rn :

Rattus norvegicus (brown rat)

Sc :

Saccharomyces cerevisiae (bakers’ yeast)

sHSP:

Small heat shock protein

Ta :

Triticum aestivum (wheat)

Tsp :

Taenia saginata (beef tapeworm)

Xa :

Xanthomonas axoponidis

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Acknowledgments

We are very grateful for the stimulating interactions we have had with all of our collaborators in the study of sHSPs, and thank all of the Benesch group for helpful discussion. We thank the Wellcome Trust (GRH, FS), the European Molecular Biology Organization (HL, AJB), European Union 7th Framework Program “PROSPECTS” (FS), Canadian Institutes of Health Research (AJB), and the Royal Society (JLPB).

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Authors and Affiliations

  1. Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK

    Gillian R. Hilton, Hadi Lioe, Florian Stengel & Justin L. P. Benesch

  2. Departments of Molecular Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, ON, Canada

    Andrew J. Baldwin

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  1. Gillian R. Hilton
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  2. Hadi Lioe
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  3. Florian Stengel
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  5. Justin L. P. Benesch
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Correspondence to Justin L. P. Benesch .

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  1. Dept. Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom

    Sophie Jackson

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Hilton, G.R., Lioe, H., Stengel, F., Baldwin, A.J., Benesch, J.L.P. (2012). Small Heat-Shock Proteins: Paramedics of the Cell. In: Jackson, S. (eds) Molecular Chaperones. Topics in Current Chemistry, vol 328. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2012_324

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