Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe
Mycobiology
;
: 272-279, 2015.
Artigo
em Inglês
| WPRIM
| ID: wpr-729636
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Piridoxina
/
Schizosaccharomyces
/
Espectrometria de Massas
/
Proteínas Recombinantes
/
Programas de Rastreamento
/
Citrato (si)-Sintase
/
Chaperonas Moleculares
/
Alfa-Cristalinas
/
Eletroforese
/
Proteínas de Choque Térmico Pequenas
Tipo de estudo:
Estudo diagnóstico
/
Estudo de rastreamento
Idioma:
Inglês
Revista:
Mycobiology
Ano de publicação:
2015
Tipo de documento:
Artigo
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