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Nucleic Acids Research Advance Access published online on August 28, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm607
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNA

Nathalie Lancelot1, Gaëlle Charier1, Joël Couprie1, Isabelle Duband-Goulet2, Béatrice Alpha-Bazin3, Eric Quémeneur3, Emilie Ma1, Marie-Claude Marsolier-Kergoat1, Virginie Ropars4, Jean-Baptiste Charbonnier1, Simona Miron5, Constantin T. Craescu5, Isabelle Callebaut6, Bernard Gilquin1 and Sophie Zinn-Justin1,*

1Institut de Biologie et Technologies de Saclay, CEA Saclay, 91191 Gif-sur-Yvette, 2Institut Jacques Monod, CNRS et Université Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, 3Institut de Biologie Environnementale et de Biotechnologie, CEA VALRHO, 30207 Bagnols-sur-Ceze, 4CNRS, UMR5048, Centre de Biochimie Structurale, 34090 Montpellier; INSERM, U554, 34090 Montpellier; Université Montpellier 1 et 2, 34090 Montpellier, 5INSERM U759 & Institut Curie-Centre de Recherche, Centre Universitaire, Bâtiment 112, 91405 Orsay and 6IMPMC, UMR 7590 Universités Paris 6 et Paris 7, 140 rue de Lourmel, 75015 Paris, France

*To whom correspondence should be addressed. Tel: +33 169083026; Fax: +33 169084712; Email: sophie.zinn{at}cea.fr

Received April 30, 2007. Revised July 26, 2007. Accepted July 26, 2007.

DNA damage checkpoints are signal transduction pathways that are activated after genotoxic insults to protect genomic integrity. At the site of DNA damage, ‘mediator’ proteins are in charge of recruiting ‘signal transducers’ to molecules ‘sensing’ the damage. Budding yeast Rad9, fission yeast Crb2 and metazoan 53BP1 are presented as mediators involved in the activation of checkpoint kinases. Here we show that, despite low sequence conservation, Rad9 exhibits a tandem tudor domain structurally close to those found in human/mouse 53BP1 and fission yeast Crb2. Moreover, this region is important for the resistance of Saccharomyces cerevisiae to different genotoxic stresses. It does not mediate direct binding to a histone H3 peptide dimethylated on K79, nor to a histone H4 peptide dimethylated on lysine 20, as was demonstrated for 53BP1. However, the tandem tudor region of Rad9 directly interacts with single-stranded DNA and double-stranded DNAs of various lengths and sequences through a positively charged region absent from 53BP1 and Crb2 but present in several yeast Rad9 homologs. Our results argue that the tandem tudor domains of Rad9, Crb2 and 53BP1 mediate chromatin binding next to double-strand breaks. However, their modes of chromatin recognition are different, suggesting that the corresponding interactions are differently regulated.


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