Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/37712
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | A specific subdomain in 29 DNA polymerase confers both processivity and strand displacement capacity |
Autor: | Rodríguez García, Irene CSIC; Lázaro, José M. CSIC; Blanco, Luis CSIC ORCID ; Kamtekar, S.; Berman, Andrea J.; Wang, J.; Steitz, T. A.; Salas, Margarita CSIC ORCID ; Vega, Miguel de CSIC ORCID | Palabras clave: | Protein-primed replication Terminal protein region Helicase-like activity DNA-binding stability |
Fecha de publicación: | 3-may-2005 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences 102: 6407-6412 (2005) | Resumen: | Recent crystallographic studies of φ29 DNA polymerase have provided structural insights into its strand displacement and processivity. A specific insertion named terminal protein region 2 (TPR2), present only in protein-primed DNA polymerases, together with the exonuclease, thumb, and palm subdomains, forms two tori capable of interacting with DNA. To analyze the functional role of this insertion, we constructed a φ29 DNA polymerase deletion mutant lacking TPR2 amino acid residues Asp-398 to Glu-420. Biochemical analysis of the mutant DNA polymerase indicates that its DNA-binding capacity is diminished, drastically decreasing its processivity. In addition, removal of the TPR2 insertion abolishes the intrinsic capacity of φ29 DNA polymerase to perform strand displacement coupled to DNA synthesis. Therefore, the biochemical results described here directly demonstrate that TPR2 plays a critical role in strand displacement and processivity. | Versión del editor: | http://dx.doi.org/10.1073/pnas.0500597102 | URI: | http://hdl.handle.net/10261/37712 | DOI: | 10.1073/pnas.0500597102 | ISSN: | 0027-8424 |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
PNAS-2005-Rodríguez-6407-12[1].pdf | 488,96 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
49
checked on 14-mar-2024
SCOPUSTM
Citations
77
checked on 14-mar-2024
WEB OF SCIENCETM
Citations
71
checked on 25-feb-2024
Page view(s)
310
checked on 19-mar-2024
Download(s)
31
checked on 19-mar-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.