ArticleNucleic acids research2006
Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- DNA Polymerases for Whole Genome Amplification: Considerations and Future Directions.International journal of molecular sciences · 2023Review
- Disclosing early steps of protein-primed genome replication of the Gram-positive tectivirus Bam35.Nucleic acids research · 2016Article
- Insights into the Determination of the Templating Nucleotide at the Initiation of φ29 DNA Replication.The Journal of biological chemistry · 2015Article
- Role of the LEXE motif of protein-primed DNA polymerases in the interaction with the incoming nucleotide.The Journal of biological chemistry · 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
- The essential role of the 3' terminal template base in the first steps of protein-primed DNA replication.PloS one · 2012Article
- Bacteriophage protein-protein interactions.Advances in virus research · 2012Review
- The mitochondrial genome of the pathogenic yeast Candida subhashii: GC-rich linear DNA with a protein covalently attached to the 5' termini.Microbiology (Reading, England) · 2010Article
- 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
- Involvement of phage phi29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication.Nucleic acids research · 2007Article
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4 authors.
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Abstract
This paper shows that the protein-primed DNA polymerases encoded by bacteriophages Nf and GA-1, unlike other DNA polymerases, do not require unwinding or processivity factors for efficient synthesis of full-length terminal protein (TP)-DNA. Analysis of their polymerization activity shows that both DNA polymerases base their replication efficiency on a high processivity and on the capacity to couple polymerization to strand displacement. Both enzymes are endowed with a proofreading activity that acts coordinately with the polymerization one to edit polymerization errors. Additionally, Nf double-stranded DNA binding protein (DBP) greatly stimulated the in vitro formation of the TP-dAMP initiation complex by decreasing the K(m) value for dATP of the Nf DNA polymerase by >20-fold. Whereas Nf DNA polymerase, as the phi29 enzyme, is able to use its homologous TP as well as DNA as primer, GA-1 DNA polymerase appears to have evolved to use its corresponding TP as the only primer of DNA synthesis. Such exceptional behaviour is discussed in the light of the recently solved structure of the DNA polymerase/TP complex of the related bacteriophage phi29.
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