Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe
Mycobiology
;
: 272-279, 2015.
Article
in English
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pyridoxine
/
Schizosaccharomyces
/
Mass Spectrometry
/
Recombinant Proteins
/
Mass Screening
/
Citrate (si)-Synthase
/
Molecular Chaperones
/
Alpha-Crystallins
/
Electrophoresis
/
Heat-Shock Proteins, Small
Type of study:
Diagnostic study
/
Screening study
Language:
English
Journal:
Mycobiology
Year:
2015
Type:
Article
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