Evidence map›Paper›PMID 35338218›Full record

ArticleScientific reports2022

The inner side of yeast PCNA contributes to genome stability by mediating interactions with Rad18 and the replicative DNA polymerase δ.

Robert Toth, Miklos Halmai, Zsuzsanna Gyorfy, Eva Balint, Ildiko Unk

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 54% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 1 country.

Robert Toth *The Institute of Genetics, Biological Research Centre, Szeged, Eotvos Loránd Research Network, Szeged, 6726, Hungary.
Miklos Halmai *The Institute of Genetics, Biological Research Centre, Szeged, Eotvos Loránd Research Network, Szeged, 6726, Hungary.
Zsuzsanna GyorfyThe Institute of Genetics, Biological Research Centre, Szeged, Eotvos Loránd Research Network, Szeged, 6726, Hungary.
Eva BalintThe Institute of Genetics, Biological Research Centre, Szeged, Eotvos Loránd Research Network, Szeged, 6726, Hungary.
Ildiko UnkThe Institute of Genetics, Biological Research Centre, Szeged, Eotvos Loránd Research Network, Szeged, 6726, Hungary. unk.ildiko@brc.hu.
Institute of Genetics · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PCNA is a central orchestrator of cellular processes linked to DNA metabolism. It is a binding platform for a plethora of proteins and coordinates and regulates the activity of several pathways. The outer side of PCNA comprises most of the known interacting and regulatory surfaces, whereas the residues at the inner side constitute the sliding surface facing the DNA double helix. Here, by investigating the L154A mutation found at the inner side, we show that the inner surface mediates protein interactions essential for genome stability. It forms part of the binding site of Rad18, a key regulator of DNA damage tolerance, and is required for PCNA sumoylation which prevents unscheduled recombination during replication. In addition, the L154 residue is necessary for stable complex formation between PCNA and the replicative DNA polymerase δ. Hence, its absence increases the mutation burden of yeast cells due to faulty replication. In summary, the essential role of the L154 of PCNA in guarding and maintaining stable replication and promoting DNA damage tolerance reveals a new connection between these processes and assigns a new coordinating function to the central channel of PCNA.

Indexed as

DNA Polymerase IIIDNADNA-Binding ProteinsDNA DamageDNA ReplicationGenomic InstabilityHumansProliferating Cell Nuclear AntigenSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesDNADNA-Binding ProteinsDNA Polymerase IIIPOL30 protein, S cerevisiaeProliferating Cell Nuclear AntigenRAD18 protein, humanRAD18 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID35338218
PMCPMC8956578
OpenAlexW4220725526

What Socratic holds

Textmetadata
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 Socratic graph.