title: Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe.
abstract: To screen molecular chaperones similar to small heat shock proteins (sHsps), but without α-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 α-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℃ 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 α-crystalline domain in their sequences.
authors.affiliation: Department of Food and Nutrition, Chonnam National University, Gwangju 61186, Korea.
authors.forename: Jiyoung
authors.initials: J
authors.lastname: Han
authors.affiliation: Department of Food and Nutrition, Chonnam National University, Gwangju 61186, Korea.
authors.forename: Kanghwa
authors.initials: K
authors.lastname: Kim
authors.affiliation: Department of Food and Nutrition, Dongshin University, Naju 58245, Korea.
authors.forename: Songmi
authors.initials: S
authors.lastname: Lee
keywords: Chaperone; Cofilin; NTF2; Schizosaccharomyces pombe; Small heat-shock proteins; Snz1; Wos2; α-Crystalline domain