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J. Biol. Chem., Vol. 281, Issue 20, 13857-13860, May 19, 2006
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Cernunnos Interacts with the XRCC4·DNA-ligase IV Complex and Is Homologous to the Yeast Nonhomologous End-joining Factor Nej1*
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From the
Département de Biologie Structurale, Institut de Minéralogie et de Physique des Milieux Condensés, CNRS UMR7590, Universités Paris 6 et Paris 7, Paris, F-75005 France, the INSERM, Hôpital Necker-Enfants Malades, U768, UnitéDéveloppement Normal et Pathologique du Système Immunitaire, Paris, F-75015 France, the ¶Université Paris Descartes, Faculté de Médecine René Descartes, Paris, F-75005 France, and the ||Assistance Publique-Hôpitaux de Paris, Hôpital Necker-Enfants Malades, Unité d'Immunologie et d'Hématologie, Paris F-75015, France
DNA double strand breaks are considered as the most harmful DNA lesions and are repaired by either homologous recombination or nonhomologous end joining (NHEJ). A new NHEJ factor, Cernunnos, has been identified, the defect of which leads to a severe immunodeficiency condition associated with microcephaly and other developmental defects in humans. This presentation is reminiscent to that of DNA-ligase IV deficiency and suggests a possible interplay between Cernunnos and the XRCC4·DNA-ligase IV complex. We show here that Cernunnos physically interacts with the XRCC4·DNA-ligase IV complex. Moreover, a combination of sensitive methods of sequence analysis revealed that Cernunnos can be associated with the XRCC4 family of proteins and that it corresponds to the genuine homolog of the yeast Nej1 protein. Altogether these results shed new lights on the last step, the DNA religation, of the NHEJ pathway.
Received for publication, December 20, 2005 , and in revised form, March 28, 2006.
* This work was supported by institutional grants from INSERM as well as grants from the Ligue National contre le Cancer (Equipe Labellisée LA LIGUE 2005, EL2005.LNCC/JPDV1), the Commissariat à l'Energie Atomique (LRC-CEA No. 40V), and the INCa/Cancéropôle IdF. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental data and Figs. S1 and S2.
1 These authors contributed equally to the work.
3 Supported by Ministere de l'Education Nationale, de l'Enseignement Supérieur, et de la Recherche.
2 To whom correspondence may be addressed: Dépt. de Biologie Structurale, IMPMC, CNRS UMR 7590, Universités Paris 6 et Paris 7, case 115, 4 place Jussieu, 75252 Paris Cedex 05, France. Tel.: 33-1-44-27-45-87; Fax: 33-1-44-27-37-85; E-mail: IsabelleCallebaut{at}impmc.jussieu.fr. 5 To whom correspondence may be addressed: INSERM U768, Hôpital Necker-Enfants Malades, 149 rue de Sèvres, 75015 Paris, France. Tel.: 33-1-44-49-50-81; Fax: 33-1-42-73-06-40; E-mail: devillar{at}necker.fr.
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