Evidence map›Paper›PMID 21112870›Full record

ArticleNucleic acids research2011

Differential modes of DNA binding by mismatch uracil DNA glycosylase from Escherichia coli: implications for abasic lesion processing and enzyme communication in the base excision repair pathway.

Seden Grippon, Qiyuan Zhao, Tom Robinson, Jacqueline J T Marshall, Rory J O'Neill, Hugh Manning, Gordon Kennedy, Christopher Dunsby, Mark Neil, Stephen E Halford and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. The response of Escherichia coli to the alkylating agents chloroacetaldehyde and styrene oxide.Mutation research. Genetic toxicology and environmental mutagenesis · 2019
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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

12 authors at 1 institution in 1 country.

Seden GripponDivision of Molecular Biosciences, Sir Alexander Fleming Building, Chemical Biology Centre, Imperial College London, South Kensington, London, SW7 2AZ, UK.
Qiyuan Zhao
Tom Robinson
Jacqueline J T Marshall
Rory J O'Neill
Hugh Manning
Gordon Kennedy
Christopher Dunsby
Mark Neil
Stephen E Halford
Paul M W French
Geoff S Baldwin
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E000495/1
6 · The paper itself

Abstract

Mismatch uracil DNA glycosylase (Mug) from Escherichia coli is an initiating enzyme in the base-excision repair pathway. As with other DNA glycosylases, the abasic product is potentially more harmful than the initial lesion. Since Mug is known to bind its product tightly, inhibiting enzyme turnover, understanding how Mug binds DNA is of significance when considering how Mug interacts with downstream enzymes in the base-excision repair pathway. We have demonstrated differential binding modes of Mug between its substrate and abasic DNA product using both band shift and fluorescence anisotropy assays. Mug binds its product cooperatively, and a stoichiometric analysis of DNA binding, catalytic activity and salt-dependence indicates that dimer formation is of functional significance in both catalytic activity and product binding. This is the first report of cooperativity in the uracil DNA glycosylase superfamily of enzymes, and forms the basis of product inhibition in Mug. It therefore provides a new perspective on abasic site protection and the findings are discussed in the context of downstream lesion processing and enzyme communication in the base excision repair pathway.

Indexed as

DNA RepairBinding, CompetitiveDNADNA DamageEscherichia coliEscherichia coli ProteinsFluorescence PolarizationProtein BindingSodium ChlorideThymine DNA GlycosylaseUracil-DNA GlycosidaseDNAEscherichia coli Proteinsmismatch-specific thymine uracil-DNA glycosylaseSodium ChlorideThymine DNA GlycosylaseUracil-DNA Glycosidase

Identifiers

PMID21112870
PMCPMC3074160
OpenAlexW2163988262

What OpenQuestion holds

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LicenceCC BY-NC
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.