Mycobiology

The Korean Society of Mycology (한국균학회)
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Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe

  • Han, Jiyoung (Department of Food and Nutrition, Chonnam National University) ;
  • Kim, Kanghwa (Department of Food and Nutrition, Chonnam National University) ;
  • Lee, Songmi (Department of Food and Nutrition, Dongshin University)
  • Received : 2015.08.13
  • Accepted : 2015.09.21
  • Published : 2015.09.30
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Abstract

To screen molecular chaperones similar to small heat shock proteins (sHsps), but without ${\alpha}$-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an ${\alpha}$-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at $70^{\circ}C$ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no ${\alpha}$-crystalline domain in their sequences.

Keywords

References

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