tRNA 2'-phosphotransferase 1 (TRPT1)

tRNA 2'-phosphotransferase 1 (TRPT1) is an enzyme that catalyzes the final step of tRNA splicing by transferring the splice junction 2'-phosphate from ligated tRNA to NAD+, producing ADP-ribose-1'',2''-cyclic phosphate[4][3]. In eukaryotes, TRPT1 is involved in posttranscriptional modification critical for tRNA maturation and function, and has also been shown to mediate ADP-ribosylation of various RNA molecules, which affects RNA stability and translation[1]. While TRPT1 is essential in certain organisms, such as fungi—making it an attractive antifungal target—it is non-essential in mammalian cells under standard laboratory conditions, though it supports cell survival and proliferation. Mutations or dysfunction in this enzyme are associated with pontocerebellar hypoplasia, and its activities are structurally conserved across species[2][3][1]. No approved drugs currently target TRPT1, but it has been proposed as a novel target for antifungal therapy based on its unique role in fungal RNA processing[2].

Other names

tRNA phosphotransferase 1TRNA phosphotransferase 1tRNA splicing 2'-phosphotransferase 1MGC11134TRPT1_HUMANtRNA 2'-phosphotransferase 1

Not established for drugs (no known direct inhibitors in clinical use); antifungal discovery proposed based on essentiality in fungal tRNA splicing[2]