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Model Chaperones: Small Heat Shock Proteins from Plants

  • Chapter
The Big Book on Small Heat Shock Proteins

Part of the book series: Heat Shock Proteins ((HESP,volume 8))

Abstract

Small heat shock proteins (sHSPs) are ubiquitous stress proteins proposed to act as ATP-independent molecular chaperones to prevent irreversible aggregation of stress-labile proteins. sHSPs range in size from ~12 to 42 kDa, but typically assemble into 12 to >32 subunit oligomers. The monomers are defined by a conserved α-crystallin domain flanked by divergent and flexible N-terminal and C-terminal arms. In higher plants sHSPs have evolved independently of metazoan and bacterial homologs and comprise multiple families of cytosolic proteins, along with proteins targeted to the nucleus, chloroplasts, mitochondria, endoplasmic reticulum and peroxisomes. This diversity of sHSPs is unique to land plants and likely arose as a result of their frequent exposure to stress due to their sessile nature. The availability of the high resolution structure of a dodecameric cytosolic class I sHSP from wheat, Ta16.9 (PDB ID: 1GME; 2.7 Å resolution), has facilitated detailed in vitro studies of sHSP chaperone action. A working model proposes that sHSP oligomers dissociate into dimers during heat stress, revealing hydrophobic patches that interact with exposed hydrophobic regions on denaturing substrates, maintaining them in a soluble, folding-competent state. sHSP-substrate complexes are then acted on by ATP-dependent chaperones to restore substrates to their native state. However, much remains to be done to connect this model with the function of the many different sHSPs found in plants. Further genetic and biochemical studies are needed to identify sHSP substrates and to define the mechanism by which sHSPs function, not only during stress, but also during specific developmental stages in plants.

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Abbreviations

ACD:

Alpha-crystallin domain

AKRA2:

Ankyrin repeat containing protein 2A (UniProt accession: Q9SAR5)

At14.7:

Arabidopsis thaliana heat shock protein 14.7 (UnitProt accession: Q6NLV0)

At15.7:

Arabidopsis thaliana heat shock protein 15.7 (UniProt accession: Q9FHQ3)

At17.4:

Arabidopsis thaliana heat shock protein 17.4 (SwissProt accession: Q9SYG1)

At17.7:

Arabidopsis thaliana heat shock protein 17.7 (UniProt accession: O81822)

At17.8:

Arabidopsis thaliana heat shock protein 17.8 (UniProt accession: Q9LNW0)

At18.5:

Arabidopsis thaliana heat shock protein 18.5 (UniProt accession: O64564)

At21.7:

Arabidopsis thaliana heat shock protein 21.7 (UniProt accession: Q9FIT9)

At22.0:

Arabidopsis thaliana heat shock protein 22.0 (UniProt accession: Q38806)

At23.5:

Arabidopsis thaliana heat shock protein 23.5 (UniProt accession: Q9FGM9)

At23.6:

Arabidopsis thaliana heat shock protein 23.6 (UniProt accession: Q96331)

At26.5:

Arabidopsis thaliana heat shock protein 26.5 (UnitProt accession: Q9SSQ8)

C. elegans :

Caenorhabditis elegans

Dr17.7:

Deinococcus radiodurans heat shock protein 17.7 (UniProt accession: Q9RTR5)

Dr20.2:

Deinococcus radiodurans heat shock protein 20.2 (UniProt accession: Q9RVB5)

EPR:

Electron paramagnetic resonance

ER:

Endoplasmic reticulum

FRET:

Förster (or fluorescence) resonance energy transfer

GST:

Glutathione-S-transferase

HSP:

Heat shock protein

MALDI-TOF:

Matrix assisted laser desorption ionization – time of flight

MI:

Mitochondrial class I small heat shock protein

MII:

Mitochondrial class II small heat shock protein

Mj16.5:

Methanocaldococcus jannaschii heat shock protein 16.5 (UniProt accession: Q57733)

NtHsp24.6:

Nicotiana tabacum heat shock protein 24.6

OEP7:

Outer envelope protein 7 (chloroplast) (UnitProt accession: Q9SVC4)

Ps17.7:

Pisum sativum heat shock protein 17.7 (UniProt accession: P19242)

Ps18.1:

Pisum sativum heat shock protein 18.1 (UniProt accession: P19243)

Sc26:

Saccharomyces cerevisiae heat shock protein 26 (UniProt accession: P15992)

sHSP:

Small heat shock protein

Sp16.0:

Schizosaccharomyces pombe heat shock protein 16.0 (UniProt accession: O14368)

Syn16.6:

Synechocystis heat shock protein 16.6 (Unit Prot accession: M1LDX9)

Ta16.9:

Triticum asetivum heat shock protein 16.9 (UniProt accession: P12810)

Ta17.8:

Triticum asetivum heat shock protein 17.8 (UniProt accession: Q94KM0)

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Acknowledgements

E. V. would like to acknowledge long term support for work on sHSP biochemistry and function from the National Institutes of Health GM RO142762, as well as support from the National Science Foundation and United States Department of Agriculture competitive grants program for studies of sHSPs in plants and the Department of Energy Basic Bioenergy Sciences program for work on the interaction of plant sHSPs and Hsp101. We also thank many lab members and colleagues for critical and productive collaborations over many years.

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Authors and Affiliations

  1. Life Science Laboratories, Department of Biochemistry and Molecular Biology, University of Massachusetts, 240 Thatcher Road, Amherst, MA, 01003, USA

    Indu Santhanagopalan, Keith N. Ballard, Nathen E. Bopp & Elizabeth Vierling

  2. Botany Department, College of Science, Tanta University, Tanta, Egypt

    Eman Basha

  3. Biology Department, Faculty of Science, Taif University, Taif, Saudi Arabia

    Eman Basha

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  1. Indu Santhanagopalan
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Correspondence to Elizabeth Vierling .

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  1. Department of Molecular Biology, Medical Biochemistry & Pathology Medical School Lab Cell & Developmental Genetics IBIS, Université Laval, Quebec, Québec, Canada

    Robert M. Tanguay

  2. Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA

    Lawrence E. Hightower

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Santhanagopalan, I., Basha, E., Ballard, K.N., Bopp, N.E., Vierling, E. (2015). Model Chaperones: Small Heat Shock Proteins from Plants. In: Tanguay, R., Hightower, L. (eds) The Big Book on Small Heat Shock Proteins. Heat Shock Proteins, vol 8. Springer, Cham. https://doi.org/10.1007/978-3-319-16077-1_5

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