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Article

Mutations of the Yku80 C terminus and Xrs2 FHA domain specifically block yeast nonhomologous end joining.

Molecular and cellular biology - 1 Dec 2005

Palmbos Phillip L, Daley James M, Wilson Thomas E

Abstract excerpt

The nonhomologous end-joining (NHEJ) pathway of DNA double-strand break repair requires three protein complexes in Saccharomyces cerevisiae: MRX (Mre11-Rad50-Xrs2), Ku (Ku70-Ku80), and DNA ligase IV (Dnl4-Lif1-Nej1). Much is known about the interactions that mediate the formation of each complex, but little is known about how they act together during repair. A comprehensive yeast two-hybrid screen of the NHEJ...

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Identifiers

PMID: 16314503
DOI: 10.1128/MCB.25.24.10782-10790.2005
PMCID: PMC1316971

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutations of the Yku80 C terminus and Xrs2 FHA domain specifically block yeast nonhomologous end joining.PMID 16314503Read ↗

Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2 FHA domain.Semantic proximity Read ↗

Non‐homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair processSemantic proximity Read ↗

Ku DNA End-Binding Activity Promotes Repair Fidelity and Influences End-Processing During Nonhomologous End-Joining in Saccharomyces cerevisiae.Semantic proximity Read ↗

Identification of a Saccharomyces cerevisiae Ku80 homologue: roles in DNA double strand break rejoining and in telomeric maintenance.Semantic proximity Read ↗

The MRX Complex Ensures NHEJ Fidelity through Multiple Pathways Including Xrs2-FHA-Dependent Tel1 Activation.Semantic proximity Read ↗

Yeast DNA ligase IV mutations reveal a nonhomologous end joining function of BRCT1 distinct from XRCC4/Lif1 binding.Semantic proximity Read ↗

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Identification of Genes Involved in Repair of DNA Double-Strand Breaks in Mammalian CellsSemantic proximity Read ↗

Di- and tri-methylation of histone H3K36 play distinct roles in DNA double-strand break repairSemantic proximity Read ↗

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