XLF and APLF bind Ku80 at two remote sites to ensure DNA repair by non-homologous end joining
The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of th...
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| Veröffentlicht in: | Nature structural & molecular biology Jg. 25; H. 10; S. 971 - 980 |
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| Abstract | The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of the NHEJ proteins APLF (A-KBM) and XLF (X-KBM) bound to a Ku-DNA complex. The two KBM motifs bind remote sites of the Ku80 α/β domain. The X-KBM occupies an internal pocket formed by an unprecedented large outward rotation of the Ku80 α/β domain. We observe independent recruitment of the APLF-interacting protein XRCC4 and of XLF to laser-irradiated sites via binding of A- and X-KBMs, respectively, to Ku80. Finally, we show that mutation of the X-KBM and A-KBM binding sites in Ku80 compromises both the efficiency and accuracy of end joining and cellular radiosensitivity. A- and X-KBMs may represent two initial anchor points to build the intricate interaction network required for NHEJ. |
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| AbstractList | The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of the NHEJ proteins APLF (A-KBM) and XLF (X-KBM) bound to a Ku-DNA complex. The two KBM motifs bind remote sites of the Ku80 α/β domain. The X-KBM occupies an internal pocket formed by an unprecedented large outward rotation of the Ku80 α/β domain. We observe independent recruitment of the APLF-interacting protein XRCC4 and of XLF to laser-irradiated sites via binding of A- and X-KBMs, respectively, to Ku80. Finally, we show that mutation of the X-KBM and A-KBM binding sites in Ku80 compromises both the efficiency and accuracy of end joining and cellular radiosensitivity. A- and X-KBMs may represent two initial anchor points to build the intricate interaction network required for NHEJ. The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of the NHEJ proteins APLF (A-KBM) and XLF (X-KBM) bound to a Ku-DNA complex. The two KBM motifs bind remote sites of the Ku80 α/β domain. The X-KBM occupies an internal pocket formed by an unprecedented large outward rotation of the Ku80 α/β domain. We observe independent recruitment of the APLF-interacting protein XRCC4 and of XLF to laser-irradiated sites via binding of A- and X-KBMs, respectively, to Ku80. Finally, we show that mutation of the X-KBM and A-KBM binding sites in Ku80 compromises both the efficiency and accuracy of end joining and cellular radiosensitivity. A- and X-KBMs may represent two initial anchor points to build the intricate interaction network required for NHEJ.The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of the NHEJ proteins APLF (A-KBM) and XLF (X-KBM) bound to a Ku-DNA complex. The two KBM motifs bind remote sites of the Ku80 α/β domain. The X-KBM occupies an internal pocket formed by an unprecedented large outward rotation of the Ku80 α/β domain. We observe independent recruitment of the APLF-interacting protein XRCC4 and of XLF to laser-irradiated sites via binding of A- and X-KBMs, respectively, to Ku80. Finally, we show that mutation of the X-KBM and A-KBM binding sites in Ku80 compromises both the efficiency and accuracy of end joining and cellular radiosensitivity. A- and X-KBMs may represent two initial anchor points to build the intricate interaction network required for NHEJ. |
| Author | Yu, Jinchao Tadi, Satish Comte, Audrey Le Cam, Eric Gontier, Amandine Drevet, Pascal Pitois, Aurelien Rothenberg, Eli Charbonnier, Jean Baptiste Ropars, Virginie Nemoz, Clement Berger, Imre Barboule, Nadia Yin, Yandong Delteil, Christine Guerois, Raphaël Baconnais, Sonia Frit, Philippe Modesti, Mauro Barbet-Massin, Emeline Calsou, Patrick Legrand, Pierre |
| Author_xml | – sequence: 1 givenname: Clement surname: Nemoz fullname: Nemoz, Clement organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 2 givenname: Virginie surname: Ropars fullname: Ropars, Virginie organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 3 givenname: Philippe surname: Frit fullname: Frit, Philippe organization: Equipe Labellisée Ligue Contre le Cancer 2018, Toulouse, France – sequence: 4 givenname: Amandine surname: Gontier fullname: Gontier, Amandine organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 5 givenname: Pascal surname: Drevet fullname: Drevet, Pascal organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 6 givenname: Jinchao orcidid: 0000-0002-5431-8298 surname: Yu fullname: Yu, Jinchao organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 7 givenname: Raphaël orcidid: 0000-0001-5294-2858 surname: Guerois fullname: Guerois, Raphaël organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 8 givenname: Aurelien surname: Pitois fullname: Pitois, Aurelien organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 9 givenname: Audrey surname: Comte fullname: Comte, Audrey organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France – sequence: 10 givenname: Christine surname: Delteil fullname: Delteil, Christine organization: Equipe Labellisée Ligue Contre le Cancer 2018, Toulouse, France – sequence: 11 givenname: Nadia surname: Barboule fullname: Barboule, Nadia organization: Equipe Labellisée Ligue Contre le Cancer 2018, Toulouse, France – sequence: 12 givenname: Pierre orcidid: 0000-0003-2431-2255 surname: Legrand fullname: Legrand, Pierre organization: Synchrotron Soleil, L'Orme des Merisiers, Saint-Aubin, Gif-sur-Yvette, France – sequence: 13 givenname: Sonia surname: Baconnais fullname: Baconnais, Sonia organization: Signalisations, Noyaux et Innovations en Cancérologie, UMR 8126, CNRS, Université Paris-Sud, Gustave Roussy, Université Paris-Saclay, Villejuif, France – sequence: 14 givenname: Yandong orcidid: 0000-0003-2499-871X surname: Yin fullname: Yin, Yandong organization: New York University School of Medicine, Perlmutter Cancer Center, New York, USA – sequence: 15 givenname: Satish surname: Tadi fullname: Tadi, Satish organization: Cancer Research Center of Marseille, CNRS UMR 7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, Marseille, France – sequence: 16 givenname: Emeline surname: Barbet-Massin fullname: Barbet-Massin, Emeline organization: Dynamic Biosensors GmbH, Martinsried, Germany – sequence: 17 givenname: Imre orcidid: 0000-0001-7518-9045 surname: Berger fullname: Berger, Imre organization: BrisSynBio Centre, School of Biochemistry, Faculty of Biomedical Sciences, University of Bristol, Bristol, UK – sequence: 18 givenname: Eric surname: Le Cam fullname: Le Cam, Eric organization: Signalisations, Noyaux et Innovations en Cancérologie, UMR 8126, CNRS, Université Paris-Sud, Gustave Roussy, Université Paris-Saclay, Villejuif, France – sequence: 19 givenname: Mauro orcidid: 0000-0002-4964-331X surname: Modesti fullname: Modesti, Mauro organization: Cancer Research Center of Marseille, CNRS UMR 7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, Marseille, France – sequence: 20 givenname: Eli surname: Rothenberg fullname: Rothenberg, Eli organization: New York University School of Medicine, Perlmutter Cancer Center, New York, USA – sequence: 21 givenname: Patrick surname: Calsou fullname: Calsou, Patrick email: calsou@ipbs.fr, calsou@ipbs.fr organization: Equipe Labellisée Ligue Contre le Cancer 2018, Toulouse, France. calsou@ipbs.fr – sequence: 22 givenname: Jean Baptiste orcidid: 0000-0002-5219-1983 surname: Charbonnier fullname: Charbonnier, Jean Baptiste email: jb.charbonnier@cea.fr organization: Institute for Integrative Biology of the Cell, Institute Joliot, CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette, France. jb.charbonnier@cea.fr |
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| Snippet | The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ)... The Ku70–Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ)... |
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| SubjectTerms | Binding sites Conserved Sequence Crystal structure Crystallography, X-Ray Deoxyribonucleic acid DNA DNA damage DNA End-Joining Repair DNA repair DNA Repair Enzymes - chemistry DNA Repair Enzymes - metabolism DNA Repair Enzymes - physiology DNA-(Apurinic or Apyrimidinic Site) Lyase - chemistry DNA-(Apurinic or Apyrimidinic Site) Lyase - metabolism DNA-(Apurinic or Apyrimidinic Site) Lyase - physiology DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology Homology Humans Ku Autoantigen - chemistry Ku Autoantigen - metabolism Ku Autoantigen - physiology Models, Molecular Molecular interactions Mutation Non-homologous end joining Poly-ADP-Ribose Binding Proteins - chemistry Poly-ADP-Ribose Binding Proteins - metabolism Poly-ADP-Ribose Binding Proteins - physiology Protein Domains Proteins Radiosensitivity Repair |
| Title | XLF and APLF bind Ku80 at two remote sites to ensure DNA repair by non-homologous end joining |
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