ReviewViruses2015
Coordinated DNA Replication by the Bacteriophage T4 Replisome.
Review in Viruses, 2015. 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, 18 citations in OpenAlex.
- Introduction.Advances in experimental medicine and biology · 2026Article
- The bacteriophage T4 replisome: a model system for understanding DNA replication mechanisms.EcoSal Plus · 2025Review
- A four-in-one replicase integrating key enzymatic activities for DNA replication.Nucleic acids research · 2025Article
- Surface-enhanced Raman spectroscopy for the characterization of bacterial pellets ofRSC advances · 2024Article
- Review
- Structure of New Binary and Ternary DNA Polymerase Complexes From Bacteriophage RB69.Frontiers in molecular biosciences · 2021Article
- Genome-wide mapping reveals conserved and diverged R-loop activities in the unusual genetic landscape of the African trypanosome genome.Nucleic acids research · 2018Article
- T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction.Nucleic acids research · 2018Article
- Investigation of sliding DNA clamp dynamics by single-molecule fluorescence, mass spectrometry and structure-based modeling.Nucleic acids research · 2018Article
- The application of thermophilic DNA primase TtDnaG2 to DNA amplification.Scientific reports · 2017Article
- A mechanistic study of helicases with magnetic traps.Protein science : a publication of the Protein Society · 2017Review
- Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the Bacteriophage T7 Replisome.Structure (London, England : 1993) · 2017Article
- Proficient Replication of the Yeast Genome by a Viral DNA Polymerase.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The T4 bacteriophage encodes eight proteins, which are sufficient to carry out coordinated leading and lagging strand DNA synthesis. These purified proteins have been used to reconstitute DNA synthesis in vitro and are a well-characterized model system. Recent work on the T4 replisome has yielded more detailed insight into the dynamics and coordination of proteins at the replication fork. Since the leading and lagging strands are synthesized in opposite directions, coordination of DNA synthesis as well as priming and unwinding is accomplished by several protein complexes. These protein complexes serve to link catalytic activities and physically tether proteins to the replication fork. Essential to both leading and lagging strand synthesis is the formation of a holoenzyme complex composed of the polymerase and a processivity clamp. The two holoenzymes form a dimer allowing the lagging strand polymerase to be retained within the replisome after completion of each Okazaki fragment. The helicase and primase also form a complex known as the primosome, which unwinds the duplex DNA while also synthesizing primers on the lagging strand. Future studies will likely focus on defining the orientations and architecture of protein complexes at the replication fork.
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Registered trials
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.