Evidence map›Paper›PMID 21764775›Full record

ArticleNucleic acids research2011

The Swi2-Snf2-like protein Uls1 is involved in replication stress response.

Magdalena Cal-Bakowska, Ireneusz Litwin, Tomasz Bocer, Robert Wysocki, Dorota Dziadkowiec

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  14. A STUbL wards off telomere fusions.The EMBO journal · 2013
    Article
  15. Review
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  17. Article
  18. Homologous recombination and its regulation.Nucleic acids research · 2012
    Review
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 1 institution in 2 countries.

Magdalena Cal-BakowskaInstitute of Plant Biology, Faculty of Biological Sciences, University of Wrocław, 50-328 Wrocław, Poland.
Ireneusz Litwin
Tomasz Bocer
Robert Wysocki
Dorota Dziadkowiec
University of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae Uls1 belongs to the Swi2-Snf2 family of DNA-dependent ATPases and a new protein family of SUMO-targeted ubiquitin ligases. Here, we examine a physiological role of Uls1 and report for the first time its involvement in response to replication stress. We found that deletion of ULS1 in cells lacking RAD52 caused a synthetic growth defect accompanied by prolonged S phase and aberrant cell morphology. uls1Δ also progressed slower through S phase upon MMS treatment and took longer to resolve replication intermediates during recovery. This suggests an important function for Uls1 during replication stress. Consistently, cells lacking Uls1 and endonuclease Mus81 were more sensitive to HU, MMS and CPT than single mus81Δ. Interestingly, deletion of ULS1 attenuated replication stress-related defects in sgs1Δ, such as sensitivity to HU and MMS while increasing the level of PCNA ubiquitination and Rad53 phosphorylation. Importantly, Uls1 interactions with Mus81 and Sgs1 were dependent on its helicase domain. We propose that Uls1 directs a subset of DNA structures arising during replication into the Sgs1-dependent pathway facilitating S phase progression. Thus, in the absence of Uls1 other modes of replication fork processing and repair are employed.

Indexed as

DNA ReplicationAdenosine TriphosphatasesDNA-Binding ProteinsDNA DamageDNA HelicasesEndonucleasesGene DeletionRad52 DNA Repair and Recombination ProteinRecQ HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsS PhaseStress, PhysiologicalUbiquitin-Protein LigasesAdenosine TriphosphatasesDNA-Binding ProteinsDNA HelicasesEndonucleasesMUS81 protein, S cerevisiaeRad52 DNA Repair and Recombination ProteinRAD52 protein, S cerevisiaeRecQ HelicasesSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiaeUbiquitin-Protein LigasesULS1 protein, S cerevisiae

Identifiers

PMID21764775
PMCPMC3203583
OpenAlexW2010784169

What OpenQuestion holds

Textmetadata
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.