Evidence map›Paper›PMID 24692662›Full record

ArticleNucleic acids research2014

Human MUS81-EME2 can cleave a variety of DNA structures including intact Holliday junction and nicked duplex.

Tamir Amangyeld, Yong-Keol Shin, Miju Lee, Buki Kwon, Yeon-Soo Seo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Cellular Responses to Widespread DNA Replication Stress.International journal of molecular sciences · 2023
    Review
  6. Review
  7. Article
  8. DNA Holliday Junction: History, Regulation and Bioactivity.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Human MUS81: A Fence-Sitter in Cancer.Frontiers in cell and developmental biology · 2021
    Review
  15. Article
  16. Review
  17. Review
  18. The Plant cell · 2018
    Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Tamir AmangyeldDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Yong-Keol ShinDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Miju LeeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Buki KwonDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.
Yeon-Soo SeoDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea yeonsooseo@kaist.ac.kr.
Korea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MUS81 shares a high-degree homology with the catalytic XPF subunit of the XPF-ERCC1 endonuclease complex. It is catalytically active only when complexed with the regulatory subunits Mms4 or Eme1 in budding and fission yeasts, respectively, and EME1 or EME2 in humans. Although Mus81 complexes are implicated in the resolution of recombination intermediates in vivo, recombinant yeast Mus81-Mms4 and human MUS81-EME1 isolated from Escherichia coli fail to cleave intact Holliday junctions (HJs) in vitro. In this study, we show that human recombinant MUS81-EME2 isolated from E. coli cleaves HJs relatively efficiently, compared to MUS81-EME1. Furthermore, MUS81-EME2 catalyzed cleavage of nicked and gapped duplex deoxyribonucleic acids (DNAs), generating double-strand breaks. The presence of a 5' phosphate terminus at nicks and gaps rendered DNA significantly less susceptible to the cleavage by MUS81-EME2 than its absence, raising the possibility that this activity could play a role in channeling damaged DNA duplexes that are not readily repaired into the recombinational repair pathways. Significant differences in substrate specificity observed with unmodified forms of MUS81-EME1 and MUS81-EME2 suggest that they play related but non-overlapping roles in DNA transactions.

Indexed as

DNA-Binding ProteinsDNA Breaks, Double-StrandedDNA Breaks, Single-StrandedDNA CleavageDNA, CruciformEndodeoxyribonucleasesEndonucleasesEscherichia coliHumansKineticsMultiprotein ComplexesProtein SubunitsSubstrate SpecificityDNA-Binding ProteinsDNA, CruciformEme1 protein, humanEME2 protein, humanEndodeoxyribonucleasesEndonucleasesMultiprotein ComplexesMUS81 protein, humanProtein Subunits

Identifiers

PMID24692662
PMCPMC4027171
OpenAlexW2141972573

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.