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Involvement of phage phi 29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication

AuthorsPérez-Arnáiz, Patricia ; Longás, Elisa ; Villar, Laurentino ; Lázaro, José M. ; Salas, Margarita ; Vega, Miguel de
KeywordsPhi 29 DNA polymerase
Phi 29 TP-DNA
Issue Date2-Oct-2007
PublisherOxford University Press
CitationNucleic Acids Research 2007 35(21):7061-7073
AbstractTo 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
Publisher version (URL)http://dx.doi.org/10.1093/nar/gkm749
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