Impact of the Potential m(6) A Modification Sites at the 3 &apos
[EN] We have previously reported the presence of m(6)A in the AMV (Alfamovirus, Bromoviridae) genome. Interestingly, two of these putative m(6)A-sites are in hairpin (hp) structures in the 3'UTR of the viral RNA3. One site ((2012)AAACU(2016)) is in the loop of hpB, within the coat protein b...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2022 |
| País: | España |
| Institución: | Universitat Politècnica de València (UPV) |
| Repositorio: | RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia |
| Idioma: | inglés |
| OAI Identifier: | oai:riunet.upv.es:10251/194257 |
| Acceso en línea: | https://riunet.upv.es/handle/10251/194257 |
| Access Level: | acceso abierto |
| Palabra clave: | N-6-methyladenosine RNA covalent modifications Plant alfamovirus DRACH motif In vivo AMV replication 3 &apos UTR BIOQUIMICA Y BIOLOGIA MOLECULAR |
| Sumario: | [EN] We have previously reported the presence of m(6)A in the AMV (Alfamovirus, Bromoviridae) genome. Interestingly, two of these putative m(6)A-sites are in hairpin (hp) structures in the 3'UTR of the viral RNA3. One site ((2012)AAACU(2016)) is in the loop of hpB, within the coat protein binding site 1 (CPB1), while the other ((1900)UGACC(1904)) is in the lower stem of hpE, a loop previously associated with AMV negative-strand RNA synthesis. In this work, we have performed in vivo experiments to assess the role of these two regions, containing the putative m(6)A-sites in the AMV cycle, by introducing compensatory point mutations to interfere with or abolish the m(6)A-tag of these sites. Our results suggest that the loop of hpB could be involved in viral replication/accumulation. Meanwhile, in the (1900)UGACC(1904) motif of the hpE, the maintenance of the adenosine residue and the lower stem hpE structure are necessary for in vivo plus-strand accumulation. These results extend our understanding of the requirements for hpE in the AMV infection cycle, indicating that both the residue identity and the base-pairing capacity in this structure are essential for viral accumulation. |
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