ArticleThe Journal of biological chemistry2007
The phage T4 protein UvsW drives Holliday junction branch migration.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.EcoSal Plus · 2025Review
- Structurally related phage helicases trigger type III-A3 retron-mediated anti-phage defense across diverse tailed phage families.Nucleic acids research · 2025Article
- Genome organisation and comparative genomics of four novel Wolbachia genome assemblies from Indian Drosophila host.Functional & integrative genomics · 2019Article
- Genome-wide relationship between R-loop formation and antisense transcription in Escherichia coli.Nucleic acids research · 2018Article
- Bacteriophage T5 gene D10 encodes a branch-migration protein.Scientific reports · 2016Article
- Irc3 is a mitochondrial DNA branch migration enzyme.Scientific reports · 2016Article
- Recombination and replication.Cold Spring Harbor perspectives in biology · 2014Review
- A structure-specific nucleic acid-binding domain conserved among DNA repair proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.Intrinsically disordered proteins · 2014Article
- Overexpression of Twinkle-helicase protects cardiomyocytes from genotoxic stress caused by reactive oxygen species.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Interaction of T4 UvsW helicase and single-stranded DNA binding protein gp32 through its carboxy-terminal acidic tail.Journal of molecular biology · 2013Article
- Improved methods for creating migratable Holliday junction substrates.Nucleic acids research · 2013Article
- RecG and UvsW catalyse robust DNA rewinding critical for stalled DNA replication fork rescue.Nature communications · 2013Article
- Direct observation of stalled fork restart via fork regression in the T4 replication system.Science (New York, N.Y.) · 2012Article
- Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW.Journal of molecular biology · 2011Article
- Assembly and dynamics of the bacteriophage T4 homologous recombination machinery.Virology journal · 2010Review
- Analysis of the DNA translocation and unwinding activities of T4 phage helicases.Methods (San Diego, Calif.) · 2010Article
- Replication fork reversal and the maintenance of genome stability.Nucleic acids research · 2009Review
- Fork regression is an active helicase-driven pathway in bacteriophage T4.EMBO reports · 2009Article
- Processive and unidirectional translocation of monomeric UvsW helicase on single-stranded DNA.Biochemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The phage T4 UvsW protein has been shown to play a crucial role in the switch from origin-dependent to recombination-dependent replication in T4 infections through the unwinding of origin R-loop initiation intermediates. UvsW also functions with UvsX and UvsY to repair damaged DNA through homologous recombination, and, based on genetic evidence, has been proposed to act as a Holliday junction branch migration enzyme. Here we report the purification and characterization of UvsW. Using oligonucleotide-based substrates, we confirm that UvsW unwinds branched DNA substrates, including X and Y structures, but shows little activity in unwinding linear duplex substrates with blunt or single-strand ends. Using a novel Holliday junction-containing substrate, we also demonstrate that UvsW promotes the branch migration of Holliday junctions efficiently through more than 1000 bp of DNA. The ATP hydrolysis-deficient mutant protein, UvsW-K141R, is unable to promote Holliday junction branch migration. However, both UvsW and UvsW-K141R are capable of stabilizing Holliday junctions against spontaneous branch migration when ATP is not present. Using two-dimensional agarose gel electrophoresis we also show that UvsW acts on T4-generated replication intermediates, including Holliday junction-containing X-shaped intermediates and replication fork-shaped intermediates. Taken together, these results strongly support a role for UvsW in the branch migration of Holliday junctions that form during T4 recombination, replication, and repair.
Indexed as
Identifiers
What OpenQuestion holds
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.