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http://dx.doi.org/10.5941/MYCO.2015.43.3.272

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)
Publication Information
Mycobiology / v.43, no.3, 2015 , pp. 272-279 More about this Journal
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
${\alpha}$-Crystalline domain; Chaperone; Cofilin; NTF2; Schizosaccharomyces pombe; Small heat-shock proteins; Snz1; Wos2;
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