||3-[(3S)-3-amino-3-carboxypropyl]uridine (acp3U) is a highly conserved modification found in tRNA core region in bacteria and eukaryotes that confers thermal stability on tRNA. The enzyme from the bacterium Escherichia coli catalyses the modification of uridine47 in the V-loop of tRNAs for Arg2, Ile1, Ile2, Ile2v, Lys, Met, Phe, Val2A, and Val2B. The human homologs DTWD1 and DTWD2 are responsible for acp3U formation at positions 20 and 20a, respectively, in the D-loop of several cytoplasmic tRNAs.
||Nishimura, S., Taya, Y., Kuchino, Y. and Ohashi, Z. 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. Biochem. Biophys. Res. Commun. 57 (1974) 702–708. [DOI] [PMID: 4597321]
||Takakura, M., Ishiguro, K., Akichika, S., Miyauchi, K. and Suzuki, T. Biogenesis and functions of aminocarboxypropyluridine in tRNA. Nat. Commun. 10:5542 (2019). [DOI] [PMID: 31804502]
||Meyer, B., Immer, C., Kaiser, S., Sharma, S., Yang, J., Watzinger, P., Weiss, L., Kotter, A., Helm, M., Seitz, H.M., Kotter, P., Kellner, S., Entian, K.D. and Wohnert, J. Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme responsible for acp3U formation at position 47 in Escherichia coli tRNAs. Nucleic Acids Res. 48 (2020) 1435–1450. [DOI] [PMID: 31863583]