Evidence map›Paper›PMID 36577401›Full record

ArticleMolecular cell2023

Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions.

Matthias Rotheneder, Kristina Stakyte, Erik van de Logt, Joseph D Bartho, Katja Lammens, Yilan Fan, Aaron Alt, Brigitte Kessler, Christophe Jung, Wynand P Roos and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.3field-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

43 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  6. Asymmetrical recognition and processing of double-strand breaks formed during DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  10. Review
  11. Article
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  13. Article
  14. Differential expression of a disease-associatedbioRxiv : the preprint server for biology · 2025
    Article
  15. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  16. Review
  17. Review
  18. ATM priming and end resection-coupled phosphorylation of MRE11 is important for fork protection and replication restart.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. NBS1 facilitates preribosomal RNA biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Matthias RothenederGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Kristina StakyteGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Erik van de LogtGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Joseph D BarthoGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Katja LammensGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Yilan FanGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Aaron AltGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Brigitte KesslerGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Christophe JungGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany.
Wynand P RoosInstitute for Toxicology, Johannes-Gutenberg-Universität, Mainz, Germany.
Barbara SteigenbergerMass Spectrometry Core Facility, Max-Planck-Institute of Biochemistry, Martinsried, Germany.
Karl-Peter HopfnerGene Center, Department of Biochemistry, Ludwig Maximilians Universität, Munich, Germany. Electronic address: hopfner@genzentrum.lmu.de.
Ludwig-Maximilians-Universität München · DEJohannes Gutenberg University Mainz · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DNA double-strand break repair complex Mre11-Rad50-Nbs1 (MRN) detects and nucleolytically processes DNA ends, activates the ATM kinase, and tethers DNA at break sites. How MRN can act both as nuclease and scaffold protein is not well understood. The cryo-EM structure of MRN from Chaetomium thermophilum reveals a 2:2:1 complex with a single Nbs1 wrapping around the autoinhibited Mre11 nuclease dimer. MRN has two DNA-binding modes, one ATP-dependent mode for loading onto DNA ends and one ATP-independent mode through Mre11's C terminus, suggesting how it may interact with DSBs and intact DNA. MRNs two 60-nm-long coiled-coil domains form a linear rod structure, the apex of which is assembled by the two joined zinc-hook motifs. Apices from two MRN complexes can further dimerize, forming 120-nm spanning MRN-MRN structures. Our results illustrate the architecture of MRN and suggest how it mechanistically integrates catalytic and tethering functions.

Indexed as

DNADNA RepairAcid Anhydride HydrolasesAdenosine TriphosphateCell Cycle ProteinsCryoelectron MicroscopyDNA Breaks, Double-StrandedDNA Repair EnzymesMRE11 Homologue ProteinAcid Anhydride HydrolasesAdenosine TriphosphateCell Cycle ProteinsDNADNA Repair EnzymesMRE11 Homologue Proteincoiled-coil domaincryo-EMDNA damage signalingDNA double-strand breaksDNA protein interactionsDNA repairX-ray crystallographyzinc-hook

Identifiers

PMID36577401
OpenAlexW4313252443

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.