The C-terminal domain of Cernunnos/XLF is dispensable for DNA repair in vivo.
The core nonhomologous end-joining DNA repair pathway is composed of seven factors: Ku70, Ku80, DNA-PKcs, Artemis, XRCC4 (X4), DNA ligase IV (L4), and Cernunnos/XLF (Cernunnos). Although Cernunnos and X4 are structurally related and participate in the same complex together with L4, they have distinct functions during DNA repair. L4 relies on X4 but not on Cernunnos for its stability, and L4 is required for optimal interaction of Cernunnos with X4. We demonstrate here, using in vitro-generated Cernunnos mutants and a series of functional assays in vivo, that the C-terminal region of Cernunnos is dispensable for its activity during DNA repair.
Malivert
Laurent
L
INSERM U768, Malades, U768, Unité de Développement Normal et Pathologique du Système Immunitaire, Hopital Necker-Enfants Malades, 149, rue de Sevres, 75015 Paris, France.
Callebaut
Isabelle
I
Rivera-Munoz
Paola
P
Fischer
Alain
A
Mornon
Jean-Paul
JP
Revy
Patrick
P
de Villartay
Jean-Pierre
JP
D000595:Amino Acid Sequence; D000072481:DNA Ligase ATP; D011088:DNA Ligases; D004260:DNA Repair; D045643:DNA Repair Enzymes / Q000737:chemistry / Q000502:physiology*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D046912:Multiprotein Complexes; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins; D017434:Protein Structure, Tertiary
D004268:DNA-Binding Proteins; C000607893:LIG4 protein, human; D046912:Multiprotein Complexes; D050505:Mutant Proteins; C508551:NHEJ1 protein, human; D011088:DNA Ligases; D045643:DNA Repair Enzymes; D000072481:DNA Ligase ATP