Evidence map›Paper›PMID 28397787›Full record

ArticleScientific reports2017

Correlated Mutation in the Evolution of Catalysis in Uracil DNA Glycosylase Superfamily.

Bo Xia, Yinling Liu, Jose Guevara, Jing Li, Celeste Jilich, Ye Yang, Liangjiang Wang, Brian N Dominy, Weiguo Cao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.0field-weighted citation impact, top 25% 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, 12 citations in OpenAlex.

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  6. Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018
    Review
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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

9 authors at 1 institution in 1 country.

Bo XiaDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Yinling LiuDepartment of Chemistry, Clemson University, 367 Hunter Laboratories, Clemson, SC 29634, USA.
Jose GuevaraDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Jing LiDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Celeste JilichDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Ye YangDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Liangjiang WangDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Brian N DominyDepartment of Chemistry, Clemson University, 367 Hunter Laboratories, Clemson, SC 29634, USA.
Weiguo CaoDepartment of Genetics and Biochemistry, Clemson University, Rooms 049 and 051 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Clemson University · US

Funding

New Enzymes for DNA DemethylationR15GM121997 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2017 to 2017
$457k
Xanthine DNA Glycosylase in Mammalian SystemsR15GM090141 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2010 to 2010
$223k
NIGMS NIH HHS R15 GM090141NIGMS NIH HHS R15 GM121997
6 · The paper itself

Abstract

Enzymes in Uracil DNA glycosylase (UDG) superfamily are essential for the removal of uracil. Family 4 UDGa is a robust uracil DNA glycosylase that only acts on double-stranded and single-stranded uracil-containing DNA. Based on mutational, kinetic and modeling analyses, a catalytic mechanism involving leaving group stabilization by H155 in motif 2 and water coordination by N89 in motif 3 is proposed. Mutual Information analysis identifies a complexed correlated mutation network including a strong correlation in the EG doublet in motif 1 of family 4 UDGa and in the QD doublet in motif 1 of family 1 UNG. Conversion of EG doublet in family 4 Thermus thermophilus UDGa to QD doublet increases the catalytic efficiency by over one hundred-fold and seventeen-fold over the E41Q and G42D single mutation, respectively, rectifying the strong correlation in the doublet. Molecular dynamics simulations suggest that the correlated mutations in the doublet in motif 1 position the catalytic H155 in motif 2 to stabilize the leaving uracilate anion. The integrated approach has important implications in studying enzyme evolution and protein structure and function.

Indexed as

BiocatalysisBiological EvolutionMultigene FamilyAmino Acid SequenceAmino Acid SubstitutionBinding SitesKineticsModels, MolecularMutant ProteinsMutationSequence AlignmentSubstrate SpecificityThermus thermophilusUracilUracil-DNA GlycosidaseMutant ProteinsUracilUracil-DNA Glycosidase

Identifiers

PMID28397787
PMCPMC5387724
OpenAlexW2607425138

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Registered trials

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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.