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Preheating induced homogeneity of the small heat shock protein fromMethanococcus jannaschii

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
1570-9639
Publisher
Elsevier
Publication Date
Volume
1784
Issue
3
Identifiers
DOI: 10.1016/j.bbapap.2007.12.008
Keywords
  • Heat Shock Protein
  • Chaperone
  • Protein Folding
  • Homogeneity
  • Hsp 16.5
Disciplines
  • Biology
  • Physics

Abstract

Abstract Small heat shock proteins usually exhibit increased chaperone-like activity either at high temperatures or after preheating. However, the activation mechanism is still unclear. In the current study, we investigated the preheating-activation process of Mj HSP16.5, using various biophysical methods. Although Mj HSP16.5 was reported to be the most monodispersed sHSPs, we found that the newly purified Mj HSP16.5 was actually heterogeneous. 85 °C-preheating could activate Mj HSP16.5 and turn it into a more compact homogeneous species at the same time. Different cooling rates after preheating did not change the activity of Mj HSP16.5, suggesting that the 85 °C-preheated Mj HSP16.5 is in the most active and also the most stable state. These results demonstrate that the activation process of Mj HSP16.5 might accompany a refolding process.

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