Biogenesis and functions of aminocarboxypropyluridine in tRNA.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31804502.
- Also identified by DOI 10.1038/s41467-019-13525-3 and PMC identifier 6895100.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Transfer (t)RNAs contain a wide variety of post-transcriptional modifications, which play critical roles in tRNA stability and functions. 3-(3-amino-3-carboxypropyl)uridine (acp<sup>3</sup>U) is a highly conserved modification found in variable- and D-loops of tRNAs. Biogenesis and functions of acp<sup>3</sup>U have not been extensively investigated. Using a reverse-genetic approach supported by comparative genomics, we find here that the Escherichia coli yfiP gene, which we rename tapT (tRNA aminocarboxypropyltransferase), is responsible for acp<sup>3</sup>U formation in tRNA. Recombinant TapT synthesizes acp<sup>3</sup>U at position 47 of tRNAs in the presence of S-adenosylmethionine. Biochemical experiments reveal that acp<sup>3</sup>U47 confers thermal stability on tRNA. Curiously, the ΔtapT strain exhibits genome instability under continuous heat stress. We also find that the human homologs of tapT, DTWD1 and DTWD2, are responsible for acp<sup>3</sup>U formation at positions 20 and 20a of tRNAs, respectively. Double knockout cells of DTWD1 and DTWD2 exhibit growth retardation, indicating that acp<sup>3</sup>U is physiologically important in mammals.
Medical subject headings
- Nucleic Acid Conformation
- RNA, Bacterial
- RNA, Transfer
- Uridine