Evidence map›Paper›PMID 26682798›Full record

ArticleNucleic acids research2016

The spliceosome-associated protein Nrl1 suppresses homologous recombination-dependent R-loop formation in fission yeast.

Lucia Aronica, Torben Kasparek, David Ruchman, Yamile Marquez, Lubos Cipak, Ingrid Cipakova, Dorothea Anrather, Barbora Mikolaskova, Maximilian Radtke, Sovan Sarkar and 8 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Dysfunction of Gpl1-Gih35-Wdr83 Complex inInternational journal of molecular sciences · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

18 authors at 6 institutions in 4 countries.

Lucia AronicaDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna A-1030, Austria Department of Oncology, Stanford University, Stanford 94305, USA timothy.humphrey@oncology.ox.ac.uk.
Torben KasparekCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK.
David RuchmanDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna A-1030, Austria.
Yamile MarquezDepartment of Medical Biochemistry, Max F. Perutz Laboratories,Medical University of Vienna, Vienna A-1030, Austria.
Lubos CipakCancer Research Institute, Slovak Academy of Sciences, Bratislava 81438, Slovakia.
Ingrid CipakovaCancer Research Institute, Slovak Academy of Sciences, Bratislava 81438, Slovakia.
Dorothea AnratherMax F. Perutz Laboratories, Mass Spectrometry Facility, Vienna A-1030, Austria.
Barbora MikolaskovaCancer Research Institute, Slovak Academy of Sciences, Bratislava 81438, Slovakia.
Maximilian RadtkeDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna A-1030, Austria.
Sovan SarkarCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK.
Chen-Chun PaiCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK.
Elizabeth BlaikleyCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK.
Carol WalkerCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK.
Kuo-Fang ShenUniversity of Southern California, Los Angeles 90089-0911, USA.
Renee SchroederDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna A-1030, Austria.
Andrea BartaDepartment of Medical Biochemistry, Max F. Perutz Laboratories,Medical University of Vienna, Vienna A-1030, Austria.
Susan L ForsburgUniversity of Southern California, Los Angeles 90089-0911, USA.
Timothy C HumphreyCRUK/MRC Oxford Institute for Radiation Oncology, Oxford OX37DQ , UK timothy.humphrey@oncology.ox.ac.uk.
CRUK/MRC Oxford Institute for Radiation Oncology · GBMax Perutz Labs · ATCancer Research Institute of the Slovak Academy of Sciences · SKUniversity of Southern California · USMedical University of Vienna · ATSlovak Academy of Sciences · SK

Funding

Genetic Analysis of MSM Protein Function in S. PombeR01GM059321 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORSBURG, SUSAN L · 1999 to 2012
$4.7M
Structural instability and DNA rearrangements in the centromereR01GM111040 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORSBURG, SUSAN L · 2014 to 2015
$626k
Austrian Science Fund FWF T 527Cancer Research UK H3RPUX00Medical Research Council MC PC 12003Medical Research Council MC_PC_12003NIGMS NIH HHS R01-GM059321NIGMS NIH HHS R01 GM111040NIGMS NIH HHS R01-GM111040
6 · The paper itself

Abstract

The formation of RNA-DNA hybrids, referred to as R-loops, can promote genome instability and cancer development. Yet the mechanisms by which R-loops compromise genome instability are poorly understood. Here, we establish roles for the evolutionarily conserved Nrl1 protein in pre-mRNA splicing regulation, R-loop suppression and in maintaining genome stability. nrl1Δ mutants exhibit endogenous DNA damage, are sensitive to exogenous DNA damage, and have defects in homologous recombination (HR) repair. Concomitantly, nrl1Δ cells display significant changes in gene expression, similar to those induced by DNA damage in wild-type cells. Further, we find that nrl1Δ cells accumulate high levels of R-loops, which co-localize with HR repair factors and require Rad51 and Rad52 for their formation. Together, our findings support a model in which R-loop accumulation and subsequent DNA damage sequesters HR factors, thereby compromising HR repair at endogenously or exogenously induced DNA damage sites, leading to genome instability.

Indexed as

Alternative SplicingDNADNA RepairGenomic InstabilityHomologous RecombinationRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRNARNA PrecursorsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpliceosomesDNANrl1 protein, S pombeRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, humanRNARNA PrecursorsSchizosaccharomyces pombe Proteins

Identifiers

PMID26682798
PMCPMC4770224
OpenAlexW2269805131

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.