Synthesis and investigation of the 5-formylcytidine modified, anticodon stem and loop of the human mitochondrial tRNAMet

• Published in: Nucleic acids research Vol. 36; no. 20; pp. 6548 - 6557
• Main Authors: Lusic, Hrvoje, Gustilo, Estella M, Vendeix, Franck A.P, Kaiser, Rob, Delaney, Michael O, Graham, William D, Moye, Virginia A, Cantara, William A, Agris, Paul F, Deiters, Alexander
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.11.2008
• Subjects: Anticodon - chemistry; Base Sequence; Codon - metabolism; Cytidine - analogs & derivatives; Cytidine - chemistry; Humans; Molecular Sequence Data; Nucleic Acid Conformation; Protein Biosynthesis; RNA; RNA - chemistry; RNA, Transfer, Met - chemical synthesis; RNA, Transfer, Met - chemistry; RNA, Transfer, Met - metabolism; Thermodynamics
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/gkn703

Human mitochondrial methionine transfer RNA (hmtRNA[Formula: see text]) has a unique post-transcriptional modification, 5-formylcytidine, at the wobble position-34 (f⁵C₃₄). The role of this modification in (hmtRNA[Formula: see text]) for the decoding of AUA, as well as AUG, in both the peptidyl- and aminoacyl-sites of the ribosome in either chain initiation or chain elongation is still unknown. We report the first synthesis and analyses of the tRNA's anticodon stem and loop domain containing the 5-formylcytidine modification. The modification contributes to the tRNA's anticodon domain structure, thermodynamic properties and its ability to bind codons AUA and AUG in translational initiation and elongation.