Evidence map›Paper›PMID 29925516›Full record

ArticleThe EMBO journal2018

The MRX complex regulates Exo1 resection activity by altering DNA end structure.

Elisa Gobbini, Corinne Cassani, Jacopo Vertemara, Weibin Wang, Fabiana Mambretti, Erika Casari, Patrick Sung, Renata Tisi, Giuseppe Zampella, Maria Pia Longhese

Abstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
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  8. Article
  9. Article
  10. Review
  11. Dynamic Properties of the DNA Damage Response Mre11/Rad50 Complex.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. MRN complex is an essential effector of DNA damage repair.Journal of Zhejiang University. Science. B · 2021
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 2 institutions in 2 countries.

Elisa GobbiniDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Corinne CassaniDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Jacopo VertemaraDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Weibin WangDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT, USA.
Fabiana MambrettiDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Erika CasariDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Patrick SungDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT, USA.
Renata TisiDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Giuseppe ZampellaDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.
Maria Pia LongheseDipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy mariapia.longhese@unimib.it.ORCID 0000-0003-1726-2034
University of Milano-Bicocca · ITYale University · US

Funding

Roles of the RecQ Helicases BLM and RECQ5 in Genome MaintenanceR01ES015632 · NIEHS · YALE UNIVERSITY · PI SUNG, PATRICK · 2007 to 2017
$3.9M
NIEHS NIH HHS R01 ES015632
6 · The paper itself

Abstract

Homologous recombination is triggered by nucleolytic degradation (resection) of DNA double-strand breaks (DSBs). DSB resection requires the Mre11-Rad50-Xrs2 (MRX) complex, which promotes the activity of Exo1 nuclease through a poorly understood mechanism. Here, we describe the Mre11-R10T mutant variant that accelerates DSB resection compared to wild-type Mre11 by potentiating Exo1-mediated processing. This increased Exo1 resection activity leads to a decreased association of the Ku complex to DSBs and an enhanced DSB resection in G1, indicating that Exo1 has a direct function in preventing Ku association with DSBs. Molecular dynamics simulations show that rotation of the Mre11 capping domains is able to induce unwinding of double-strand DNA (dsDNA). The R10T substitution causes altered orientation of the Mre11 capping domain that leads to persistent melting of the dsDNA end. We propose that MRX creates a specific DNA end structure that promotes Exo1 resection activity by facilitating the persistence of this nuclease on the DSB ends, uncovering a novel MRX function in DSB resection.

Indexed as

DNA Breaks, Double-StrandedDNA, FungalEndodeoxyribonucleasesExodeoxyribonucleasesMultiprotein ComplexesProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalEndodeoxyribonucleasesexodeoxyribonuclease IExodeoxyribonucleasesMRE11 protein, S cerevisiaeMultiprotein ComplexesSaccharomyces cerevisiae Proteinsdouble‐strand breakExo1MRXresectionSae2

Identifiers

PMID29925516
PMCPMC6092625
OpenAlexW2808942117

What OpenQuestion holds

Textmetadata
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.