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Article

Two-step mechanism and step-arrest mutants of Runella slithyformis NAD+-dependent tRNA 2'-phosphotransferase Tpt1.

RNA (New York, N.Y.) - 1 Sept 2018

Munir Annum, Abdullahu Leonora, Damha Masad J, Shuman Stewart

Abstract excerpt

Tpt1 catalyzes the transfer of an internal 2'-monophosphate moiety (2'-PO4) from a "branched" 2'-PO4 RNA splice junction to NAD+ to form a "clean" 2'-OH, 3'-5' phosphodiester junction, ADP-ribose 1″-2″ cyclic phosphate, and nicotinamide. First discovered as an essential component of the Saccharomyces cerevisiae tRNA splicing machinery, Tpt1 is widely distributed in nature, including in taxa that have no...

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Identifiers

PMID: 29884622
DOI: 10.1261/rna.067165.118
PMCID: PMC6097658

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