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Título : Involvement of phage phi 29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication
Autor : Pérez-Arnáiz, Patricia ; Longás, Elisa; Villar, Laurentino; Lázaro, José M.; Salas, Margarita; Vega, Miguel de
Palabras clave : Phi 29 DNA polymerase
Phi 29 TP-DNA
Fecha de publicación : 2-oct-2007
Editor: Oxford University Press
Citación : Nucleic Acids Research 2007 35(21):7061-7073
Resumen: To initiate phi 29 DNA replication, the DNA polymerase has to form a complex with the homologous primer terminal protein (TP) that further recognizes the replication origins of the homologous TP-DNA placed at both ends of the linear genome. By means of chimerical proteins, constructed by swapping the priming domain of the related phi 29 and GA-1 TPs, we show that DNA polymerase can form catalytically active heterodimers exclusively with that chimerical TP containing the N-terminal part of the homologous TP, suggesting that the interaction between the polymerase TPR-1 subdomain and the TP N-terminal part is the one mainly responsible for the specificity between both proteins. We also show that the TP N-terminal part assists the proper binding of the priming domain at the polymerase active site. Additionally, a chimerical phi 29 DNA polymerase containing the GA-1 TPR-1 subdomain could use GA-1 TP, but only in the presence of phi 29 TP-DNA as template, indicating that parental TP recognition is mainly accomplished by the DNA polymerase. The sequential events occurring during initiation of bacteriophage protein-primed DNA replication are proposed
Versión del editor: http://dx.doi.org/10.1093/nar/gkm749
URI : http://hdl.handle.net/10261/7901
DOI: 10.1093/nar/gkm749
ISSN: 0305-1048 (print)
1362-4962 (online)
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