Publications

• Biogenesis and functions of aminocarboxypropyluridine in tRNA.

  Takakura M., Ishiguro K., Akichika S., Miyauchi K., Suzuki T.

  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 (acp³U) is a highly conserved modification found in variable- and D-loops of tRNAs. Biogenesis and functions of ac ... >> More

  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 (acp³U) is a highly conserved modification found in variable- and D-loops of tRNAs. Biogenesis and functions of acp³U 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 acp³U formation in tRNA. Recombinant TapT synthesizes acp³U at position 47 of tRNAs in the presence of S-adenosylmethionine. Biochemical experiments reveal that acp³U47 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 acp³U formation at positions 20 and 20a of tRNAs, respectively. Double knockout cells of DTWD1 and DTWD2 exhibit growth retardation, indicating that acp³U is physiologically important in mammals. << Less

  Nat. Commun. 10:5542-5542(2019) [PubMed] [EuropePMC]

• Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia coli phenylalanine transfer RNA: transfer of the 3-amino-acid-3-carboxypropyl group from S-adenosylmethionine.

  Nishimura S., Taya Y., Kuchino Y., Oashi Z.

  Biochem. Biophys. Res. Commun. 57:702-708(1974) [PubMed] [EuropePMC]

  This publication is cited by 1 other entry.

• Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme responsible for acp3U formation at position 47 in Escherichia coli tRNAs.

  Meyer B., Immer C., Kaiser S., Sharma S., Yang J., Watzinger P., Weiss L., Kotter A., Helm M., Seitz H.M., Koetter P., Kellner S., Entian K.D., Woehnert J.

  tRNAs from all domains of life contain modified nucleotides. However, even for the experimentally most thoroughly characterized model organism Escherichia coli not all tRNA modification enzymes are known. In particular, no enzyme has been found yet for introducing the acp3U modification at positio ... >> More

  tRNAs from all domains of life contain modified nucleotides. However, even for the experimentally most thoroughly characterized model organism Escherichia coli not all tRNA modification enzymes are known. In particular, no enzyme has been found yet for introducing the acp3U modification at position 47 in the variable loop of eight E. coli tRNAs. Here we identify the so far functionally uncharacterized YfiP protein as the SAM-dependent 3-amino-3-carboxypropyl transferase catalyzing this modification and thereby extend the list of known tRNA modification enzymes in E. coli. Similar to the Tsr3 enzymes that introduce acp modifications at U or m1Ψ nucleotides in rRNAs this protein contains a DTW domain suggesting that acp transfer reactions to RNA nucleotides are a general function of DTW domain containing proteins. The introduction of the acp3U-47 modification in E. coli tRNAs is promoted by the presence of the m7G-46 modification as well as by growth in rich medium. However, a deletion of the enzymes responsible for the modifications at position 46 and 47 in the variable loop of E. coli tRNAs did not lead to a clearly discernible phenotype suggesting that these two modifications play only a minor role in ensuring the proper function of tRNAs in E. coli. << Less

  Nucleic Acids Res. 48:1435-1450(2020) [PubMed] [EuropePMC]