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TitleStructural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50.
Journal, issue, pagesMol Cell, Vol. 82, Issue 18, Page 3513-33522.e6, Year 2022
Publish dateAug 12, 2022
AuthorsFabian Gut / Lisa Käshammer / Katja Lammens / Joseph D Bartho / Anna-Maria Boggusch / Erik van de Logt / Brigitte Kessler / Karl-Peter Hopfner /
PubMed AbstractDNA double-strand breaks (DSBs) threaten genome stability and are linked to tumorigenesis in humans. Repair of DSBs requires the removal of attached proteins and hairpins through a poorly understood ...DNA double-strand breaks (DSBs) threaten genome stability and are linked to tumorigenesis in humans. Repair of DSBs requires the removal of attached proteins and hairpins through a poorly understood but physiologically critical endonuclease activity by the Mre11-Rad50 complex. Here, we report cryoelectron microscopy (cryo-EM) structures of the bacterial Mre11-Rad50 homolog SbcCD bound to a protein-blocked DNA end and a DNA hairpin. The structures reveal that Mre11-Rad50 bends internal DNA for endonucleolytic cleavage and show how internal DNA, DNA ends, and hairpins are processed through a similar ATP-regulated conformational state. Furthermore, Mre11-Rad50 is loaded onto blocked DNA ends with Mre11 pointing away from the block, explaining the distinct biochemistries of 3' → 5' exonucleolytic and endonucleolytic incision through the way Mre11-Rad50 interacts with diverse DNA ends. In summary, our results unify Mre11-Rad50's enigmatic nuclease diversity within a single structural framework and reveal how blocked DNA ends and hairpins are processed.
External linksMol Cell / PubMed:35987200
MethodsEM (single particle)
Resolution3.4 - 8.2 Å
Structure data

14391

7yzo

EMDB-14391, PDB-7yzo:
Endonuclease state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and dsDNA
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-14392: Composite map of two E. coli Mre11-Rad50 (SbcCD) complexes bound to Ku70/80 blocked dsDNA in endonuclease state
Method: EM (single particle) / Resolution: 8.2 Å

14393

7yzp

EMDB-14393, PDB-7yzp:
Hairpin-bound state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and a DNA hairpin
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-14394: C. thermophilum Ku70/80 heterodimer bound to DNA
Method: EM (single particle) / Resolution: 3.5 Å

14403

7z03

EMDB-14403, PDB-7z03:
Endonuclease state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and extended dsDNA
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-MN:
Unknown entry

Source
  • escherichia coli (E. coli)
  • synthetic construct (others)
  • Chaetomium thermophilum (fungus)
  • DNA molecule (others)
  • Chaetomium ther (E. coli)
KeywordsDNA BINDING PROTEIN / ABC-type ATPase / Nuclease / DNA repair

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