Evidence map›Paper›PMID 19208629›Full record

ArticleThe Journal of biological chemistry2009

Stimulation of UvrD helicase by UvrAB.

John Atkinson, Colin P Guy, Chris J Cadman, Geri F Moolenaar, Nora Goosen, Peter McGlynn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024
    Review
  2. Article
  3. Article
  4. Regulation of UvrD Helicase Activity by MutL.Journal of molecular biology · 2018
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Protein-DNA complexes are the primary sources of replication fork pausing in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Prokaryotic nucleotide excision repair.Cold Spring Harbor perspectives in biology · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Interaction of Rep and DnaB on DNA.Nucleic acids research · 2011
    Article
  16. Article
  17. DNA Helicases.EcoSal Plus · 2010
    Article
  18. 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

6 authors at 2 institutions in 2 countries.

John AtkinsonSchool of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.
Colin P Guy
Chris J Cadman
Geri F Moolenaar
Nora Goosen
Peter McGlynn
University of Aberdeen · GBLeiden University · NL

Funding

Biotechnology and Biological Sciences Research Council BB/C008316/1Medical Research Council G0501626
6 · The paper itself

Abstract

Helicases play critical roles in all aspects of nucleic acid metabolism by catalyzing the remodeling of DNA and RNA structures. UvrD is an abundant helicase in Escherichia coli with well characterized functions in mismatch and nucleotide excision repair and a possible role in displacement of proteins such as RecA from single-stranded DNA. The mismatch repair protein MutL is known to stimulate UvrD. Here we show that the nucleotide excision repair proteins UvrA and UvrB can together stimulate UvrD-catalyzed unwinding of a range of DNA substrates containing strand discontinuities, including forked DNA substrates. The stimulation is specific for UvrD, as UvrAB failed to stimulate Rep helicase, a UvrD homologue. Moreover, although UvrAB can promote limited strand displacement, stimulation of UvrD did not require the strand displacement function of UvrAB. We conclude that UvrAB, like MutL, modulate UvrD helicase activity. This stimulation likely plays a role in DNA strand and protein displacement by UvrD in nucleotide excision repair. Promotion of UvrD-catalyzed unwinding of nicked duplexes by UvrAB may also explain the need for UvrAB and UvrD in Okazaki fragment processing in cells lacking DNA polymerase I. More generally, these data support the idea that helicase activity is regulated in vivo, with helicases acting as part of multisubunit complexes rather than in isolation.

Indexed as

Adenosine TriphosphatasesBiocatalysisDNADNA-Binding ProteinsDNA HelicasesEscherichia coliEscherichia coli ProteinsSubstrate SpecificityAdenosine TriphosphatasesDNADNA-Binding ProteinsDNA HelicasesEscherichia coli ProteinsUvrA protein, E coliUvrB protein, E coliUvrD protein, E coli

Identifiers

PMID19208629
PMCPMC2666613
OpenAlexW2017771362

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.