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pubmed-article:19622355pubmed:abstractTextPreviously we reported that in vitro translation activity in extracts of Saccharomyces cerevisiae was stimulated by dithiothreitol (DTT) and further increased by the addition of thioredoxin (TRX1) [Choi, S.K. (2007) Thioredoxin-mediated regulation of protein synthesis by redox in Saccharomyces cerevisiae. Kor. J. Microbiol. Biotechnol. 35, 36-40]. To identify the pathway affecting translation, we cloned and purified thioredoxin reductase 1 (TRR1), thioredoxin reductase 2 (TRR2), glutaredoxin 1 (GRX1) and glutaredoxin reductase 1 (GLR1) as fusion proteins. Thioredoxin-mediated activation of translation was more effectively stimulated by NADPH or NADH than by DTT. Moreover, addition of TRR1 led to a further increase of translation in the presence of thioredoxin plus NADPH. These findings indicate that redox control via the thioredoxin-thioredoxin reductase system plays an important role in the regulation of translation.lld:pubmed
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pubmed-article:19622355pubmed:articleTitleActivation of translation via reduction by thioredoxin-thioredoxin reductase in Saccharomyces cerevisiae.lld:pubmed
pubmed-article:19622355pubmed:affiliationDepartment of Biological Sciences, College of Life Industry and Science, Sunchon National University, Jeonnam, Republic of Korea.lld:pubmed
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pubmed-article:19622355pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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