Evidence map›Paper›PMID 28978435›Full record

ArticleBiophysical journal2017

Modulation of Escherichia coli UvrD Single-Stranded DNA Translocation by DNA Base Composition.

Eric J Tomko, Timothy M Lohman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Inhibition of the SARS-CoV-2 helicase at single-nucleotide resolution.bioRxiv : the preprint server for biology · 2022
    Article
  5. Sequence-dependent mechanochemical coupling of helicase translocation and unwinding at single-nucleotide resolution.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Regulation of E. coli Rep helicase activity by PriC.Journal of molecular biology · 2021
    Article
  7. Review
  8. Review
  9. Article
  10. UvrD helicase activation by MutL involves rotation of its 2B subdomain.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. 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

2 authors at 1 institution in 1 country.

Eric J TomkoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri.
Timothy M LohmanDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri. Electronic address: lohman@biochem.wustl.edu.
Washington University in St. Louis · US

Funding

HELICASE-CATALYZED DNA UNWINDINGR01GM045948 · NIGMS · WASHINGTON UNIVERSITY · PI LOHMAN, TIMOTHY M · 1991 to 2020
$9.2M
NIGMS NIH HHS R01 GM045948
6 · The paper itself

Abstract

Escherichia coli UvrD is an SF1A DNA helicase/translocase that functions in chromosomal DNA repair and replication of some plasmids. UvrD can also displace proteins such as RecA from DNA in its capacity as an anti-recombinase. Central to all of these activities is its ATP-driven 3'-5' single-stranded (ss) DNA translocation activity. Previous ensemble transient kinetic studies have estimated the average translocation rate of a UvrD monomer on ssDNA composed solely of deoxythymidylates. Here we show that the rate of UvrD monomer translocation along ssDNA is influenced by DNA base composition, with UvrD having the fastest rate along polypyrimidines although decreasing nearly twofold on ssDNA containing equal amounts of the four bases. Experiments with DNA containing abasic sites and polyethylene glycol spacers show that the ssDNA base also influences translocation processivity. These results indicate that changes in base composition and backbone insertions influence the translocation rates, with increased ssDNA base stacking correlated with decreased translocation rates, supporting the proposal that base-stacking interactions are involved in the translocation mechanism.

Indexed as

Base CompositionDNA HelicasesDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsKineticsPolyethylene GlycolsPurinesPyrimidinesDNA HelicasesDNA, Single-StrandedEscherichia coli ProteinsPolyethylene GlycolsPurinesPyrimidinesUvrD protein, E coli

Identifiers

PMID28978435
PMCPMC5627390
OpenAlexW2763021725

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.