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Activation of translation via reduction by thioredoxin–thioredoxin reductase in Saccharomyces cerevisiae
Author(s) -
Jun Kyung Ok,
Song Chin-Hee,
Kim Young-Bum,
An Jinseok,
Oh Jae Hyeun,
Choi Sang Ki
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.030
Subject(s) - glutaredoxin , thioredoxin , ferredoxin thioredoxin reductase , thioredoxin reductase , saccharomyces cerevisiae , biochemistry , dithiothreitol , reductase , chemistry , enzyme , yeast
Previously 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.