ArticleProceedings of the National Academy of Sciences of the United States of America2010
Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- Sequential membrane- and protein-bound organelles compartmentalize genomes during phage infection.Cell host & microbe · 2025Article
- Autoregulation ensures vertical transmission of the linear prophage GIL01.Communications biology · 2024Article
- A transcriptionally active lipid vesicle encloses the injectedbioRxiv : the preprint server for biology · 2024Article
- Engineered bacterial orthogonal DNA replication system for continuous evolution.Nature chemical biology · 2023Article
- Replication Compartments of Eukaryotic and Bacterial DNA Viruses: Common Themes Between Different Domains of Host Cells.Annual review of virology · 2022Review
- Bacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-associated HU proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Temporal compartmentalization of viral infection in bacterial cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Phage Nucleus and PhuZ Spindle: Defining Features of the Subcellular Organization and Speciation of Nucleus-Forming Jumbo Phages.Frontiers in microbiology · 2021Review
- My scientific life.Bacteriophage · 2016Article
- 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
- A prophage-encoded actin-like protein required for efficient viral DNA replication in bacteria.Nucleic acids research · 2015Article
- Dissecting the role of the ϕ29 terminal protein DNA binding residues in viral DNA replication.Nucleic acids research · 2015Article
- Improved artificial origins for phage Φ29 terminal protein-primed replication. Insights into early replication events.Nucleic acids research · 2014Article
- The effect of inhibition of host MreB on the infection of thermophilic phage GVE2 in high temperature environment.Scientific reports · 2014Article
- Phage 29 phi protein p1 promotes replication by associating with the FtsZ ring of the divisome in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- My life with bacteriophage phi29.The Journal of biological chemistry · 2012Article
- 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
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism leading to protein-primed DNA replication has been studied extensively in vitro. However, little is known about the in vivo organization of the proteins involved in this fundamental process. Here we show that the terminal proteins (TPs) of phages ϕ29 and PRD1, infecting the distantly related bacteria Bacillus subtilis and Escherichia coli, respectively, associate with the host bacterial nucleoid independently of other viral-encoded proteins. Analyses of phage ϕ29 revealed that the TP N-terminal domain (residues 1-73) possesses sequence-independent DNA-binding capacity and is responsible for its nucleoid association. Importantly, we show that in the absence of the TP N-terminal domain the efficiency of ϕ29 DNA replication is severely affected. Moreover, the TP recruits the phage DNA polymerase to the bacterial nucleoid, and both proteins later are redistributed to enlarged helix-like structures in an MreB cytoskeleton-dependent way. These data disclose a key function for the TP in vivo: organizing the early viral DNA replication machinery at the cell nucleoid.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.