Evidence map›Paper›PMID 29985422›Full record

ArticleScientific reports2018

The active site residues Gln55 and Arg73 play a key role in DNA damage bypass by S. cerevisiae Pol η.

Elizaveta O Boldinova, Artem Ignatov, Andrey Kulbachinskiy, Alena V Makarova

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. The Catalytic Activity of Human REV1 on Undamaged and Damaged DNA.International journal of molecular sciences · 2024
    Article
  3. 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

4 authors at 3 institutions in 1 country.

Elizaveta O BoldinovaInstitute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 2, 123182, Moscow, Russia.
Artem IgnatovInstitute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 2, 123182, Moscow, Russia.
Andrey KulbachinskiyInstitute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 2, 123182, Moscow, Russia.
Alena V MakarovaInstitute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 2, 123182, Moscow, Russia. amakarova-img@yandex.ru.
Russian Academy of Sciences · RUInstitute of Molecular Genetics · RUKurchatov Institute · RU

Funding

Russian Foundation for Basic Research (RFBR) 15-04-08398-aRussian Foundation for Basic Research (RFBR) 15-34-70002-моs-a
6 · The paper itself

Abstract

Eukaryotic DNA polymerase eta (Pol η) plays a key role in the efficient and accurate DNA translesion synthesis (TLS) opposite UV-induced thymine dimers. Pol η is also involved in bypass of many other DNA lesions but possesses low fidelity on undamaged DNA templates. To better understand the mechanism of DNA synthesis by Pol η we investigated substitutions of evolutionary conserved active site residues Gln55 and Arg73 in Saccharomyces cerevisiae Pol η. We analyzed the efficiency and fidelity of DNA synthesis by the mutant Pol η variants opposite thymine dimers, abasic site, thymine glycol, 8-oxoguanine and on undamaged DNA. Substitutions Q55A and R73A decreased the catalytic activity and significantly affected DNA damage bypass by Pol η. In particular, the Q55A substitution reduced the efficiency of thymine dimers bypass, R73A had a stronger effect on the TLS-activity opposite abasic site, while both substitutions impaired replication opposite thymine glycol. Importantly, the R73A substitution also increased the fidelity of Pol η. Altogether, these results reveal a key role of residues Gln55 and Arg73 in DNA synthesis opposite various types of DNA lesions and highlight the evolutionary importance of the Pol η TLS function at the cost of DNA replication accuracy.

Indexed as

DNA RepairArginineCatalytic DomainDNA DamageDNA-Directed DNA PolymeraseDNA ReplicationGlycineGuanineMutagenesis, Site-DirectedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThymineY-Family DNA Polymerases8-hydroxyguanineArginineDNA-Directed DNA PolymeraseGlycineGuanineRad30 proteinSaccharomyces cerevisiae ProteinsThyminethymine glycolY-Family DNA Polymerases

Identifiers

PMID29985422
PMCPMC6037775
OpenAlexW2810929555

What OpenQuestion holds

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LicenceCC BY
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.