Model Chaperones: Small Heat Shock Proteins from Plants

  • Indu Santhanagopalan
  • Eman Basha
  • Keith N. Ballard
  • Nathen E. Bopp
  • Elizabeth VierlingEmail author
Part of the Heat Shock Proteins book series (HESP, volume 8)


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.


α-crystallin domain Hydrogen-deuterium exchange Nanoelectrospray mass spectrometry IxI motif Chaperone efficiency Replica exchange molecular dynamics Arabidopsis thaliana Synechocystis sp. PCC 6803 N-terminal arm Stress response Chaperone network 



Alpha-crystallin domain


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


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


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


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


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


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


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


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


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


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


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


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

C. elegans

Caenorhabditis elegans


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


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


Electron paramagnetic resonance


Endoplasmic reticulum


Förster (or fluorescence) resonance energy transfer




Heat shock protein


Matrix assisted laser desorption ionization – time of flight


Mitochondrial class I small heat shock protein


Mitochondrial class II small heat shock protein


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


Nicotiana tabacum heat shock protein 24.6


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


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


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


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


Small heat shock protein


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


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


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


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



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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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Indu Santhanagopalan
    • 1
  • Eman Basha
    • 2
    • 3
  • Keith N. Ballard
    • 1
  • Nathen E. Bopp
    • 1
  • Elizabeth Vierling
    • 1
    Email author
  1. 1.Life Science Laboratories, Department of Biochemistry and Molecular BiologyUniversity of MassachusettsAmherstUSA
  2. 2.Botany Department, College of ScienceTanta UniversityTantaEgypt
  3. 3.Biology Department, Faculty of ScienceTaif UniversityTaifSaudi Arabia

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