ArticleProceedings of the National Academy of Sciences of the United States of America2008
Phage phi29 and Nf terminal protein-priming domain specifies the internal template nucleotide to initiate DNA replication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Genome sequence of staphylococcal phage ESa4 of the genusMicrobiology resource announcements · 2025Article
- Cryo-EM Structures of Two Bacteriophage Portal Proteins Provide Insights for Antimicrobial Phage Engineering.Viruses · 2021Article
- Telomere associated primase Tap repairs truncated telomeres of Streptomyces.Nucleic acids research · 2017Article
- 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
- Diverse virulent pneumophages infect Streptococcus mitis.PloS one · 2015Article
- Article
- Functional eukaryotic nuclear localization signals are widespread in terminal proteins of bacteriophages.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Bacteriophage protein-protein interactions.Advances in virus research · 2012Review
- The essential role of the 3' terminal template base in the first steps of protein-primed DNA replication.PloS one · 2012Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophages phi29 and Nf from Bacillus subtilis start replication of their linear genome at both DNA ends by a protein-primed mechanism, by which the DNA polymerase, in a template-instructed reaction, adds 5'-dAMP to a molecule of terminal protein (TP) to form the initiation product TP-dAMP. Mutational analysis of the 3 terminal thymines of the Nf DNA end indicated that initiation of Nf DNA replication is directed by the third thymine on the template, the recovery of the 2 terminal nucleotides mainly occurring by a stepwise sliding-back mechanism. By using chimerical TPs, constructed by swapping the priming domain of the related phi29 and Nf proteins, we show that this domain is the main structural determinant that dictates the internal 3' nucleotide used as template during initiation.
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