Evidence map›Paper›PMID 9233823›Full record

ArticleThe EMBO journal1997

Bacteriophage T4 UvsW protein is a helicase involved in recombination, repair and the regulation of DNA replication origins.

K Carles-Kinch, J W George, K N Kreuzer

Abstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.3field-weighted citation impact, top 18% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
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  12. Ribonucleotides in bacterial DNA.Critical reviews in biochemistry and molecular biology · 2015
    Review
  13. 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 · 2014
    Article
  14. Article
  15. Break-induced DNA replication.Cold Spring Harbor perspectives in biology · 2013
    Review
  16. Article
  17. Article
  18. Rho-dependent transcription termination is essential to prevent excessive genome-wide R-loops in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

K Carles-KinchDuke University Medical Center, Department of Microbiology and Program in Cell and Molecular Biology, Durham, NC 27710, USA.
J W George
K N Kreuzer
Duke University · USLawrence Livermore National Laboratory · USPurdue University West Lafayette · US

Funding

INITIATION OF DNA REPLICATION IN THE PHAGE T4 SYSTEMR37GM034622 · NIGMS · DUKE UNIVERSITY · PI KREUZER, KENNETH N · 2001 to 2005
$1.5M
INITIATION OF DNA REPLICATION IN THE PHAGE T4 SYSTEMR01GM034622 · NIGMS · DUKE UNIVERSITY · PI KREUZER, KENNETH N · 1985 to 2000
$252k
THE REPAIR OF THE CLEAVABLE COMPLEX IN BACTERIOPHAGE T4F32GM015985 · NIGMS · DUKE UNIVERSITY · PI GEORGE, JAMES W · 1993 to 1995
–
NIGMS NIH HHS F32 GM15985NIGMS NIH HHS GM34622
6 · The paper itself

Abstract

Bacteriophage T4 UvsW protein is involved in phage recombination, repair and the regulation of replication origins. Here, we provide evidence that UvsW functions as a helicase. First, expression of UvsW allows growth of an (otherwise inviable) Escherichia coli recG rnhA double mutant, consistent with UvsW being a functional analog of the RecG helicase. Second, UvsW contains helicase sequence motifs, and a substitution (K141R) in the Walker 'A' motif prevents growth of the E.coli recG rnhA double mutant. Third, UvsW, but not UvsW-K141R, inhibits replication from a T4 origin at which persistent RNA-DNA hybrids form and presumably trigger replication initiation. Fourth, mutations that inactivate UvsW and endonuclease VII (which cleaves DNA branches) synergistically block repair of double-strand breaks. These in vivo results are consistent with a model in which UvsW is a DNA helicase that catalyzes branch migration and dissociation of RNA-DNA hybrids. In support of this model, a partially purified GST/UvsW fusion protein, but not a GST/UvsW-K141R fusion, displays ssDNA-dependent ATPase activity and is able to unwind a branched DNA substrate.

Indexed as

DNA RepairEscherichia coli ProteinsReplication OriginAdenosine TriphosphatasesBacterial ProteinsBacteriophage T4DNADNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesEscherichia coliGlutathione TransferaseRecombinant Fusion ProteinsRibonuclease HViral ProteinsVirus ReplicationAdenosine TriphosphatasesBacterial ProteinsDNADNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesendodeoxyribonuclease VIIEscherichia coli ProteinsGlutathione TransferaseRecG protein, E coliRecombinant Fusion ProteinsRibonuclease Hribonuclease HIUvsW protein, Bacteriophage T4Viral Proteins

Identifiers

PMID9233823
PMCPMC1170037
OpenAlexW2169323137

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.