Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/37712
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

A specific subdomain in 29 DNA polymerase confers both processivity and strand displacement capacity

AutorRodríguez 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 claveProtein-primed replication
Terminal protein region
Helicase-like activity
DNA-binding stability
Fecha de publicación3-may-2005
EditorNational Academy of Sciences (U.S.)
CitaciónProceedings of the National Academy of Sciences 102: 6407-6412 (2005)
ResumenRecent 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 editorhttp://dx.doi.org/10.1073/pnas.0500597102
URIhttp://hdl.handle.net/10261/37712
DOI10.1073/pnas.0500597102
ISSN0027-8424
Aparece en las colecciones: (CBM) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
PNAS-2005-Rodríguez-6407-12[1].pdf488,96 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

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.