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TitleRad1-Rad10 uses different interfaces to interact with pathway-specific DNA repair factors.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 17, Year 2026
Publish dateSep 7, 2026
AuthorsJavier Rodríguez González / Olivia T Herman / Kaden E Lewis / Lindsay A Matthews / Luke D Hess / Jennifer A Surtees / Alba Guarné /
PubMed AbstractSaccharomyces cerevisiae Rad1-Rad10 (XPF-ERCC1 in humans) is a 3'-flap endonuclease with key roles in DNA repair. Pathway-specific repair factors determine its recruitment to specific DNA substrates. ...Saccharomyces cerevisiae Rad1-Rad10 (XPF-ERCC1 in humans) is a 3'-flap endonuclease with key roles in DNA repair. Pathway-specific repair factors determine its recruitment to specific DNA substrates. Saw1 recruits it to 3' non-homologous tail recombination intermediates, while Rad14 recruits it to UV-lesions repaired by nucleotide excision repair. However, the exact recruitment mechanisms are unknown. We determined the cryo-EM structure of the Rad1-Rad10-Saw1 complex at 3.7 Å resolution. The structure reveals that Saw1 wraps around the helicase-like domain of Rad1 defining an extensive interface. Point mutations on this surface disrupt the interaction and inhibit double-strand break repair without compromising nucleotide excision repair, indicating that Rad1-Rad10 uses different surfaces to interact with pathway-specific repair factors. Mutational analyses confirm that Rad14 and Saw1 bind to opposite faces of Rad1. Accordingly, defects on the Rad14-binding interface disrupt nucleotide excision repair without affecting double-strand break repair. In contrast to XPF-ERCC1, Rad1-Rad10 does not adopt an auto-inhibited conformation in the absence of DNA indicating that substrate binding may be regulated differently across species. Collectively, our data provide structural insight into how targeting factors interact with Rad1-Rad10 to recruit it to different DNA repair intermediates.
External linksNucleic Acids Res / PubMed:42745665 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 4.5 Å
Structure data

75395

10qx

EMDB-75395, PDB-10qx:
Cryo-EM structure of Rad1-Rad10
Method: EM (single particle) / Resolution: 4.5 Å

75396

10qy

EMDB-75396, PDB-10qy:
Cryo-EM structure of the Rad1-Rad10-Saw1 complex
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsDNA BINDING PROTEIN / DNA repair / Structure-selective endonuclease / 3'-flap endonuclease / nucleotide excision repair / single-strand annealing / 3' NHTR

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