ArticleNucleic acids research2007
Involvement of phage phi29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The Loop of the TPR1 Subdomain of Phi29 DNA Polymerase Plays a Pivotal Role in Primer-Terminus Stabilization at the Polymerization Active Site.Biomolecules · 2019Article
- Engineering Permissive Insertion Sites in the Bacteriophage Phi29 DNA-Linked Terminal Protein.PloS one · 2016Article
- DNA-Binding Proteins Essential for Protein-Primed Bacteriophage Φ29 DNA Replication.Frontiers in molecular biosciences · 2016Review
- Insights into the Determination of the Templating Nucleotide at the Initiation of φ29 DNA Replication.The Journal of biological chemistry · 2015Article
- Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.Nucleic acids research · 2015Article
- Article
- Improved artificial origins for phage Φ29 terminal protein-primed replication. Insights into early replication events.Nucleic acids research · 2014Article
- Article
- Involvement of residues of the 29 terminal protein intermediate and priming domains in the formation of a stable and functional heterodimer with the replicative DNA polymerase.Nucleic acids research · 2012Article
- A novel replicative enzyme encoded by the linear Arthrobacter plasmid pAL1.Journal of bacteriology · 2010Article
- Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Involvement of the TPR2 subdomain movement in the activities of phi29 DNA polymerase.Nucleic acids research · 2009Article
- Phage phi29 and Nf terminal protein-priming domain specifies the internal template nucleotide to initiate DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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6 authors.
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Abstract
To initiate phi29 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 phi29 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 29 DNA polymerase containing the GA-1 TPR-1 subdomain could use GA-1 TP, but only in the presence of phi29 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.
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