Mycobiology.  2015 Sep;43(3):272-279. 10.5941/MYCO.2015.43.3.272.

Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe

• Han J
• Kim K
• Lee S

• KMID: 2312823
• DOI: http://doi.org/10.5941/MYCO.2015.43.3.272

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.

Keyword

alpha-Crystalline domain; Chaperone; Cofilin; NTF2; Schizosaccharomyces pombe; Small heat-shock proteins; Snz1; Wos2

MeSH Terms

alpha-Crystallins
Citrate (si)-Synthase
Electrophoresis
Heat-Shock Proteins, Small*
Mass Screening*
Mass Spectrometry
Molecular Chaperones*
Pyridoxine
Recombinant Proteins
Schizosaccharomyces*
Citrate (si)-Synthase
Heat-Shock Proteins, Small
Molecular Chaperones
Pyridoxine
Recombinant Proteins
alpha-Crystallins