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Bioinformatics Advance Access published online on March 7, 2006
Bioinformatics, doi:10.1093/bioinformatics/btl075
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© The Author (2006). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received January 30, 2005
Accepted February 27, 2006

Discovery note

Detection of a tandem BRCT in Nbs1 and Xrs2 with functional implications in the DNA damage response

Emmanuelle Becker 1 {sect}, Vincent Meyer 2 {sect}, Hocine Madaoui 1, and Raphaël Guerois 1 *

1 Service de Biophysique des Fonctions Membranaires, URA CNRS 2096, Département de Biologie Joliot-Curie, CEA Saclay, 91191 Gif-Sur-Yvette, Cedex, France
2 Département d'Etude et d'Ingénierie des Protéines, CEA Saclay, 91191 Gif-Sur-Yvette, Cedex, France

* To whom correspondence should be addressed.
Raphaël Guerois, E-mail: guerois{at}cea.fr


  Abstract

Motivation: Human Nbs1 and its homolog Xrs2 in S. cerevisiae are part of the conserved MRN complex (MRX in yeast) which plays a crucial role in maintaining genomic stability. NBS1 corresponds to the gene mutated in the Nijmegen breakage syndrome (NBS) known as a radiation hyper-sensitive disease. Despite the conservation and the importance of the MRN complex, the high sequence divergence between Nbs1 and Xrs2 precluded the identification of common domains downstream of the N-terminal FHA domain.

Results: Using HMM-HMM profile comparisons and structure modelling, we assessed the existence of a tandem BRCT in both Nbs1 and Xrs2 after the FHA. The structure based conservation analysis of the tandem BRCT in Nbs1 supports its function as a phosphoserine binding domain. Remarkably, the 5-base-pair deletion observed in 95% of NBS patients cleaves the tandem at the linker region while preserving the structural integrity of each BRCT domain in the resulting truncated gene products.

Supplementary information: http://www-spider.cea.fr/Groups/si6661/view.html.

{sect}both authors contributed equally to this work

Associate Editor: Anna Tramontano


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