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• W2065232441 abstract "RtcB enzymes are a newly discovered family of RNA ligases, implicated in tRNA splicing and other RNA repair reactions, that seal broken RNAs with 2′,3′-cyclic phosphate and 5′-OH ends. Parsimony and energetics would suggest a one-step mechanism for RtcB sealing via attack by the O5′ nucleophile on the cyclic phosphate, with expulsion of the ribose O2′ and generation of a 3′,5′-phosphodiester at the splice junction. Yet we find that RtcB violates Occam's razor, insofar as (i) it is adept at ligating 3′-monophosphate and 5′-OH ends; (ii) it has an intrinsic 2′,3′-cyclic phosphodiesterase activity. The 2′,3′-cyclic phosphodiesterase and ligase reactions both require manganese and are abolished by mutation of the RtcB active site. Thus, RtcB executes a unique two-step pathway of strand joining whereby the 2′,3′-cyclic phosphodiester end is hydrolyzed to a 3′-monophosphate, which is then linked to the 5′-OH end to form the splice junction. The energy for the 3′-phosphate ligase activity is provided by GTP, which reacts with RtcB in the presence of manganese to form a covalent RtcB-guanylate adduct. This adduct is sensitive to acid and hydroxylamine but resistant to alkali, consistent with a phosphoramidate bond. RtcB enzymes are a newly discovered family of RNA ligases, implicated in tRNA splicing and other RNA repair reactions, that seal broken RNAs with 2′,3′-cyclic phosphate and 5′-OH ends. Parsimony and energetics would suggest a one-step mechanism for RtcB sealing via attack by the O5′ nucleophile on the cyclic phosphate, with expulsion of the ribose O2′ and generation of a 3′,5′-phosphodiester at the splice junction. Yet we find that RtcB violates Occam's razor, insofar as (i) it is adept at ligating 3′-monophosphate and 5′-OH ends; (ii) it has an intrinsic 2′,3′-cyclic phosphodiesterase activity. The 2′,3′-cyclic phosphodiesterase and ligase reactions both require manganese and are abolished by mutation of the RtcB active site. Thus, RtcB executes a unique two-step pathway of strand joining whereby the 2′,3′-cyclic phosphodiester end is hydrolyzed to a 3′-monophosphate, which is then linked to the 5′-OH end to form the splice junction. The energy for the 3′-phosphate ligase activity is provided by GTP, which reacts with RtcB in the presence of manganese to form a covalent RtcB-guanylate adduct. This adduct is sensitive to acid and hydroxylamine but resistant to alkali, consistent with a phosphoramidate bond." @default.
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• W2065232441 date "2011-12-01" @default.
• W2065232441 modified "2023-10-05" @default.
• W2065232441 title "Novel Mechanism of RNA Repair by RtcB via Sequential 2′,3′-Cyclic Phosphodiesterase and 3′-Phosphate/5′-Hydroxyl Ligation Reactions" @default.
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• W2065232441 doi "https://doi.org/10.1074/jbc.m111.302133" @default.
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