Evidence map›Paper›PMID 15284331›Full record

ArticleNucleic acids research2004

Role of DNA polymerase eta in the bypass of abasic sites in yeast cells.

Bo Zhao, Zhongwen Xie, Huiyun Shen, Zhigang Wang

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.5field-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

44 citing papers in PubMed, 77 citations in OpenAlex.

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  12. Involvement of Rev1 in alkylating agent-induced loss of heterozygosity in Oryzias latipes.Genes to cells : devoted to molecular & cellular mechanisms · 2020
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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

4 authors at 1 institution in 1 country.

Bo ZhaoGraduate Center for Toxicology, University of Kentucky, Lexington, KY 40536, USA.
Zhongwen Xie
Huiyun Shen
Zhigang Wang
University of Kentucky · US

Funding

Mechanisms of DNA Lesion Bypass in EukaryotesR01CA092528 · NCI · UNIVERSITY OF KENTUCKY · PI WANG, ZHIGANG · 2002 to 2006
$1.2M
NCI NIH HHS CA92528NCI NIH HHS R01 CA092528
6 · The paper itself

Abstract

Abasic (AP) sites are major DNA lesions and are highly mutagenic. AP site-induced mutagenesis largely depends on translesion synthesis. We have examined the role of DNA polymerase eta (Poleta) in translesion synthesis of AP sites by replicating a plasmid containing a site-specific AP site in yeast cells. In wild-type cells, AP site bypass resulted in preferred C insertion (62%) over A insertion (21%), as well as -1 deletion (3%), and complex event (14%) containing multiple mutations. In cells lacking Poleta (rad30), Rev1, Polzeta (rev3), and both Poleta and Polzeta, translesion synthesis was reduced to 30%, 30%, 15% and 3% of the wild-type level, respectively. C insertion opposite the AP site was reduced in rad30 mutant cells and was abolished in cells lacking Rev1 or Polzeta, but significant A insertion was still detected in these mutant cells. While purified yeast Polalpha effectively inserted an A opposite the AP site in vitro, purified yeast Poldelta was much less effective in A insertion opposite the lesion due to its 3'-->5' proofreading exonuclease activity. Purified yeast Poleta performed extension synthesis from the primer 3' A opposite the lesion. These results show that Poleta is involved in translesion synthesis of AP sites in yeast cells, and suggest that an important role of Poleta is to catalyze extension following A insertion opposite the lesion. Consistent with these conclusions, rad30 mutant cells were sensitive to methyl methanesulfonate (MMS), and rev1 rad30 or rev3 rad30 double mutant cells were synergistically more sensitive to MMS than the respective single mutant strains.

Indexed as

DNA DamageBase SequenceDNA-Directed DNA PolymeraseDNA, FungalDNA Polymerase IIIExodeoxyribonucleasesFungal ProteinsGenetic VectorsMethyl MethanesulfonateModels, GeneticMutagensNucleotidyltransferasesPlasmidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemplates, GeneticDNA-Directed DNA PolymeraseDNA, FungalDNA Polymerase IIIExodeoxyribonucleasesFungal ProteinsMethyl MethanesulfonateMutagensNucleotidyltransferasesPOL3 protein, S cerevisiaeRad30 proteinREV1 protein, S cerevisiaeREV3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsY-Family DNA Polymerases

Identifiers

PMID15284331
PMCPMC506798
OpenAlexW2153845158

What OpenQuestion holds

Textmetadata
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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.