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TitleStructural basis for DNA break sensing by human MRE11-RAD50-NBS1 and its regulation by telomeric factor TRF2.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8320, Year 2025
Publish dateSep 18, 2025
AuthorsYilan Fan / Filiz Kuybu / Hengjun Cui / Katja Lammens / Jia-Xuan Chen / Michael Kugler / Christophe Jung / Karl-Peter Hopfner /
PubMed AbstractThe 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 ...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 (cryo-EM) structures of human MRN bound to DNA and to DNA and the telomere protection factor TRF2. MRN senses DSBs through a tight clamp-like sensing state with closed coiled-coil domains, but auto-inhibited MRE11 nuclease. NBS1 wraps around the MRE11 dimer, with NBS1's ATM recruitment motif sequestered by binding to the regulatory RAD50 S site, necessitating a switch in the NBS1 C helix for ATM activation. At telomeric DNA, TRF2 blocks the second S site via the iDDR motif to prevent nuclease and ATM activation. Our results provide a structural framework for DNA sensing via a gating mechanism and separation of sensing, signaling and processing activities of mammalian MRN.
External linksNat Commun / PubMed:40968163 / PubMed Central
MethodsEM (single particle)
Resolution2.59 - 3.11 Å
Structure data

52959

9q9h

EMDB-52959, PDB-9q9h:
Cryo-EM structure of human Mre11-Rad50 complex bound to DNA
Method: EM (single particle) / Resolution: 3.11 Å

52960

9q9i

EMDB-52960, PDB-9q9i:
Cryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA
Method: EM (single particle) / Resolution: 2.79 Å

52961

9q9j

EMDB-52961, PDB-9q9j:
Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric factor TRF2 fragment (438-542)
Method: EM (single particle) / Resolution: 2.71 Å

52962

9q9k

EMDB-52962, PDB-9q9k:
Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor TRF2 fragment (438-542)
Method: EM (single particle) / Resolution: 2.59 Å

52964

9q9m

EMDB-52964, PDB-9q9m:
Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric factor TRF2
Method: EM (single particle) / Resolution: 2.81 Å

EMDB-54397: Cryo-EM map of human MRE11-RAD50-NBS1 complex bound to ATPgammaS
Method: EM (single particle) / Resolution: 3.05 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Mre11-Rad50-DNA complex / double-strand DNA break repair / nuclease / Mre11-Rad50-Nbs1 complex / double-strand DNA break repair protein / Mre11-Rad50-TRF2 complex / Mre11-Rad50-Nbs1-TRF2 complex

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