Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe.
10.5941/MYCO.2015.43.3.272
- Author:
Jiyoung HAN
1
;
Kanghwa KIM
;
Songmi LEE
Author Information
1. Department of Food and Nutrition, Chonnam National University, Gwangju 61186, Korea.
- Publication Type:Original Article
- Keywords:
alpha-Crystalline domain;
Chaperone;
Cofilin;
NTF2;
Schizosaccharomyces pombe;
Small heat-shock proteins;
Snz1;
Wos2
- MeSH:
alpha-Crystallins;
Citrate (si)-Synthase;
Electrophoresis;
Heat-Shock Proteins, Small*;
Mass Screening*;
Mass Spectrometry;
Molecular Chaperones*;
Pyridoxine;
Recombinant Proteins;
Schizosaccharomyces*
- From:Mycobiology
2015;43(3):272-279
- CountryRepublic of Korea
- Language:English
-
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 70degrees 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.
