ArticleProceedings of the National Academy of Sciences of the United States of America2017
Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Torsion is a dynamic regulator of DNA replication stalling and reactivation.Nature communications · 2025Article
- A single helicase-binding domain of DnaG couples with hexameric helicase DnaB inBiophysics reports · 2025Article
- Cryo-EM reveals molecular mechanisms underlying the inhibitory effect of netrin-4 on laminin matrix formation.Nature communications · 2025Article
- Artificial intelligence and the analysis of cryo-EM data provide structural insight into the molecular mechanisms underlying LN-lamininopathies.Scientific reports · 2023Article
- Novel Artificial Intelligence-Based Approaches for Ab Initio Structure Determination and Atomic Model Building for Cryo-Electron Microscopy.Micromachines · 2023Review
- Reclassification of family A DNA polymerases reveals novel functional subfamilies and distinctive structural features.Nucleic acids research · 2023Article
- Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy.Micromachines · 2022Review
- Residues located in the primase domain of the bacteriophage T7 primase-helicase are essential for loading the hexameric complex onto DNA.The Journal of biological chemistry · 2022Article
- Review
- Review
- Combined Solution and Crystal Methods Reveal the Electrostatic Tethers That Provide a Flexible Platform for Replication Activities in the Bacteriophage T7 Replisome.Biochemistry · 2019Article
- Structural basis for adPEO-causing mutations in the mitochondrial TWINKLE helicase.Human molecular genetics · 2019Article
- Structures and operating principles of the replisome.Science (New York, N.Y.) · 2019Article
- Perturbing cohesin dynamics drives MRE11 nuclease-dependent replication fork slowing.Nucleic acids research · 2019Article
- Helicase promotes replication re-initiation from an RNA transcript.Nature communications · 2018Article
- The ring-shaped hexameric helicases that function at DNA replication forks.Nature structural & molecular biology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
We present a structure of the ∼650-kDa functional replisome of bacteriophage T7 assembled on DNA resembling a replication fork. A structure of the complex consisting of six domains of DNA helicase, five domains of RNA primase, two DNA polymerases, and two thioredoxin (processivity factor) molecules was determined by single-particle cryo-electron microscopy. The two molecules of DNA polymerase adopt a different spatial arrangement at the replication fork, reflecting their roles in leading- and lagging-strand synthesis. The structure, in combination with biochemical data, reveals molecular mechanisms for coordination of leading- and lagging-strand synthesis. Because mechanisms of DNA replication are highly conserved, the observations are relevant to other replication systems.
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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.