Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/305610
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration |
Autor: | Nguyen, Phong Quoc; Huecas, Sonia CSIC ORCID ; Asif-Laidin, Amna; Plaza-Pegueroles, Adrián CSIC ORCID; Capuzzi, Beatrice; Palmic, Noé; Conesa, Christine; Acker, Joël; Reguera, Juan; Lesage, Pascale; Fernández-Tornero, Carlos CSIC ORCID | Fecha de publicación: | 28-mar-2023 | Editor: | Springer Nature | Citación: | Nature Communications 14: 1729 (2023) | Resumen: | The yeast Ty1 retrotransposon integrates upstream of genes transcribed by RNA polymerase III (Pol III). Specificity of integration is mediated by an interaction between the Ty1 integrase (IN1) and Pol III, currently uncharacterized at the atomic level. We report cryo-EM structures of Pol III in complex with IN1, revealing a 16-residue segment at the IN1 C-terminus that contacts Pol III subunits AC40 and AC19, an interaction that we validate by in vivo mutational analysis. Binding to IN1 associates with allosteric changes in Pol III that may affect its transcriptional activity. The C-terminal domain of subunit C11, involved in RNA cleavage, inserts into the Pol III funnel pore, providing evidence for a two-metal mechanism during RNA cleavage. Additionally, ordering next to C11 of an N-terminal portion from subunit C53 may explain the connection between these subunits during termination and reinitiation. Deletion of the C53 N-terminal region leads to reduced chromatin association of Pol III and IN1, and a major fall in Ty1 integration events. Our data support a model in which IN1 binding induces a Pol III configuration that may favor its retention on chromatin, thereby improving the likelihood of Ty1 integration. | Descripción: | 13 p.-6 fig. | Versión del editor: | https://doi.org/10.1038/s41467-023-37109-4 | URI: | http://hdl.handle.net/10261/305610 | DOI: | 10.1038/s41467-023-37109-4 | E-ISSN: | 2041-1723 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Nature Communications_Nguyen_2023.pdf | Artículo principal | 3,08 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
2
checked on 28-abr-2024
WEB OF SCIENCETM
Citations
2
checked on 24-feb-2024
Page view(s)
28
checked on 03-may-2024
Download(s)
27
checked on 03-may-2024
Google ScholarTM
Check
Altmetric
Altmetric
Este item está licenciado bajo una Licencia Creative Commons