Evidence map›Paper›PMID 32341533›Full record

ArticleNature structural & molecular biology2020

Reconstitution of translesion synthesis reveals a mechanism of eukaryotic DNA replication restart.

Thomas A Guilliam, Joseph T P Yeeles

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 88 citations in OpenAlex.

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  12. DNA polymerase ζ is a robust reverse transcriptase.bioRxiv : the preprint server for biology · 2024
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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

2 authors at 1 institution in 1 country.

Thomas A GuilliamDivision of Protein and Nucleic Acid Chemistry, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0003-0065-2693
Joseph T P YeelesDivision of Protein and Nucleic Acid Chemistry, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK. jyeeles@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-2255-2119
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_1201/12Wellcome TrustWellcome Trust 213596/Z/18/Z
6 · The paper itself

Abstract

Leading-strand template aberrations cause helicase-polymerase uncoupling and impede replication fork progression, but the details of how uncoupled forks are restarted remain uncertain. Using purified proteins from Saccharomyces cerevisiae, we have reconstituted translesion synthesis (TLS)-mediated restart of a eukaryotic replisome following collision with a cyclobutane pyrimidine dimer. We find that TLS functions 'on the fly' to promote resumption of rapid replication fork rates, despite lesion bypass occurring uncoupled from the Cdc45-MCM-GINS (CMG) helicase. Surprisingly, the main lagging-strand polymerase, Pol δ, binds the leading strand upon uncoupling and inhibits TLS. Pol δ is also crucial for efficient recoupling of leading-strand synthesis to CMG following lesion bypass. Proliferating cell nuclear antigen monoubiquitination positively regulates TLS to overcome Pol δ inhibition. We reveal that these mechanisms of negative and positive regulation also operate on the lagging strand. Our observations have implications for both fork restart and the division of labor during leading-strand synthesis generally.

Indexed as

DNA ReplicationAcetyltransferasesCell Cycle ProteinsDNA-Binding ProteinsDNA Polymerase IIDNA Polymerase IIIDNA RepairMembrane ProteinsMinichromosome Maintenance ProteinsNuclear ProteinsProliferating Cell Nuclear AntigenSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Activating EnzymesUbiquitinationAcetyltransferasesCDC45 protein, S cerevisiaeCell Cycle ProteinsDNA-Binding ProteinsDNA Polymerase IIDNA Polymerase IIIELO2 protein, S cerevisiaeMembrane ProteinsMinichromosome Maintenance ProteinsMRC1 protein, S cerevisiaeNuclear ProteinsPOL30 protein, S cerevisiaeProliferating Cell Nuclear AntigenSaccharomyces cerevisiae ProteinsUba1 protein, S cerevisiaeUbiquitin-Activating Enzymes

Identifiers

PMID32341533
PMCPMC7116498
OpenAlexW3019593371

What OpenQuestion holds

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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.