Journal
CHEMBIOCHEM
Volume 19, Issue 7, Pages 687-695Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201700692
Keywords
cytochromes; desulfuration; thiouridine; tRNA; wobble position
Funding
- National Science Centre in Poland [UMO-2014/13/B/ST5/03979]
- Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences
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The 5-substituted 2-thiouridines (R5S2Us) present in the first (wobble) position of the anticodon of transfer RNAs (tRNAs) contribute to accuracy in reading mRNA codons and tuning protein synthesis. Previously, we showed that, under oxidative stress conditions in vitro, R5S2Us were sensitive to hydrogen peroxide (H2O2) and that their oxidative desulfuration produced 5-substituted uridines (R5Us) and 4-pyrimidinone nucleosides (R5H2Us) at a ratio that depended on the pH and an R5 substituent. Here, we demonstrate that the desulfuration of 2-thiouridines, either alone or within an RNA/tRNA chain, is catalyzed by cytochromec (cytc). Its kinetics are similar to those of Fenton-type catalytic 2-thiouridine (S2U) desulfuration. Cytc/H2O2- and Fe-II-mediated reactions deliver predominantly 4-pyrimidinone nucleoside (H2U)-type products. The pathway of the cytc/H2O2-peroxidase-mediated S2UH2U transformation through uridine sulfenic (U-SOH), sulfinic (U-SO2H), and sulfonic (U-SO3H) intermediates is confirmed by LC-MS. The cytc/H2O2-mediated oxidative damage of S2U-tRNA may have biological relevance through alteration of the cellular functions of transfer RNA.
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