Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.
作者： Takayuki Nakamura , Tetsuya Ohno , Kiichi Hirota , Akira Nishiyama , Hajime Nakamura
DOI: 10.1080/10715769900300931
关键词:
摘要: We have isolated a cDNA encoding glutaredoxin (GRX) from mouse splenic library. This encoded protein of 107 amino acids with calculated molecular weight 11.9 kDa. The deduced acid sequence in was highly homologous that other mammals (81–89%), containing putative active -Cys-Pro-Try-Cys-. Recombinant expressed E. coli showed glutathione-disulfide oxidoreductase activity β-hydroxyethyl disulfide as its substrate, whereas mutant (Cys 22, Cys 25 to Ser) no activity. In electrophoretic mobility shift assay, we proved wild type GRX, not one, recovered the DNA-binding transcription factor, PEBP2, oxidized by diamide. GRX may be involved redox regulation PEBP2 is case thioredoxin.
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