Article

Structural basis for DNA double-strand break sensing by human MRE11-RAD50-NBS1 and its TRF2 complex

2025-03-16

Abstract excerpt

<h4>Summary</h4> The MRE11-RAD50-NBS1 (MRN) complex is a central, multifunctional factor in the detection, signaling and nucleolytic processing of DNA double-strand breaks (DSBs). To clarify how human MRN binds generic and telomeric DNA ends and can separate DNA end sensing from nuclease activities, we determined cryo-electron microscopy structures of human MRN bound to DNA and to DNA and the telomere protection...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: d5a2d416-8076-54de-8b8e-9c0d4ff00d28
DOI: 10.1101/2025.03.14.643254

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Structural basis for DNA double-strand break sensing by human MRE11-RAD50-NBS1 and its TRF2 complexDOI 10.1101/2025.03.14.643254Read

Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repairSemantic proximity Read

Mre11–Rad50–Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin templateThis paper is one of a selection of papers published in this Special Issue, entitled 28th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.Semantic proximity Read

The MRE11–RAD50–NBS1 Complex Conducts the Orchestration of Damage Signaling and Outcomes to Stress in DNA Replication and RepairSemantic proximity Read

The MRN complex in double-strand break repair and telomere maintenance.Semantic proximity Read

Binding of the TRF2 iDDR motif to RAD50 highlights a convergent evolutionary strategy to inactivate MRN at telomeresSemantic proximity Read

MRE11-RAD50-NBS1 Complex Is Sufficient to Promote Transcription by RNA Polymerase II at Double-Strand Breaks by Melting DNA Ends.Semantic proximity Read

Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.Semantic proximity Read

The cryo-EM structure of human CST reveals a two-megadalton decameric assembly bound to telomeric DNASemantic proximity Read

Nbs1 Converts the Human Mre11/Rad50 Nuclease Complex into an Endo/Exonuclease Machine Specific for Protein-DNA Adducts.Semantic proximity Read

Molecular insights into the activation of Mre11-Rad50 endonuclease activity by Sae2/CtIPSemantic proximity Read

A Survey of Reported Disease-Related Mutations in the MRE11-RAD50-NBS1 Complex.Semantic proximity Read

Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.Semantic proximity Read