Evidence map›Paper›PMID 17251197›Full record

ArticleNucleic acids research2007

Contributions of ubiquitin- and PCNA-binding domains to the activity of Polymerase eta in Saccharomyces cerevisiae.

Joanne L Parker, Aleksandra B Bielen, Ivan Dikic, Helle D Ulrich

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 103 citations in OpenAlex.

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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 2 countries.

Joanne L ParkerCancer Research UK, London Research Institute, Clare Hall Laboratories, Blanche Lane, South Mimms, EN6 3LD, United Kingdom.
Aleksandra B Bielen
Ivan Dikic
Helle D Ulrich
Goethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bypassing of DNA lesions by damage-tolerant DNA polymerases depends on the interaction of these enzymes with the monoubiquitylated form of the replicative clamp protein, PCNA. We have analyzed the contributions of ubiquitin and PCNA binding to damage bypass and damage-induced mutagenesis in Polymerase eta (encoded by RAD30) from the budding yeast Saccharomyces cerevisiae. We report here that a ubiquitin-binding domain provides enhanced affinity for the ubiquitylated form of PCNA and is essential for in vivo function of the polymerase, but only in conjunction with a basal affinity for the unmodified clamp, mediated by a conserved PCNA interaction motif. We show that enhancement of the interaction and function in damage tolerance does not depend on the ubiquitin attachment site within PCNA. Like its mammalian homolog, budding yeast Polymerase eta itself is ubiquitylated in a manner dependent on its ubiquitin-binding domain.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesDNADNA-Binding ProteinsDNA DamageDNA-Directed DNA PolymeraseMolecular Sequence DataProliferating Cell Nuclear AntigenProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitinsY-Family DNA PolymerasesDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseProliferating Cell Nuclear AntigenRAD18 protein, S cerevisiaeRad30 proteinRAD6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitinsY-Family DNA Polymerases

Identifiers

PMID17251197
PMCPMC1807963
OpenAlexW2154462755

What OpenQuestion holds

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LicenceCC BY-NC
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.