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Synthesis and investigation of the 5-formylcytidine modified, anticodon stem and loop of the human mitochondrial tRNA(Met)

Human mitochondrial methionine transfer RNA (hmtRNA(Met)(CAU)) has a unique post-transcriptional modification, 5-formylcytidine, at the wobble position-34 (f(5)C(34)). The role of this modification in (hmtRNA(Met)(CAU)) for the decoding of AUA, as well as AUG, in both the peptidyl- and aminoacyl-sit...

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Detalles Bibliográficos
Autores principales: 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
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2008
Materias:
RNA
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582600/
https://www.ncbi.nlm.nih.gov/pubmed/18927116
http://dx.doi.org/10.1093/nar/gkn703
Descripción
Sumario:Human mitochondrial methionine transfer RNA (hmtRNA(Met)(CAU)) has a unique post-transcriptional modification, 5-formylcytidine, at the wobble position-34 (f(5)C(34)). The role of this modification in (hmtRNA(Met)(CAU)) 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.