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Nucleic Acids Research 2004 32(11):3316-3324; doi:10.1093/nar/gkh652
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Published online 22 June 2004

Nucleic Acids Research, Vol. 32 No. 11 © Oxford University Press 2004; all rights reserved

The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase ß and increases its DNA substrate utilisation efficiency: implications for DNA repair

Magali Toueille, Nazim El-Andaloussi, Isabelle Frouin, Raimundo Freire1, Dorothee Funk, Igor Shevelev, Erica Friedrich-Heineken, Giuseppe Villani2, Michael O. Hottiger and Ulrich Hübscher*

Institute of Veterinary Biochemistry and Molecular Biology, University of Zürich-Irchel, Wintherturerstrasse 190, CH-8057, Zürich, Switzerland, 1 Unidad de Investigacion, Hospital Universitario de Canarias, Ofra s/n, La Cuesta, 38320 Tenerife, Spain and 2 Institut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique, 205 Route de Narbonne, 31077 Toulouse Cedex, France

* To whom correspondence should be addressed. Tel: +33 1 635 54 72/71; Fax: +33 1 635 68 40; Email: hubscher{at}vetbio.unizh.ch

Received April 1, 2004; Revised May 25, 2004; Accepted May 26, 2004

In eukaryotic cells, checkpoints are activated in response to DNA damage. This requires the action of DNA damage sensors such as the Rad family proteins. The three human proteins Rad9, Rad1 and Hus1 form a heterotrimeric complex (called the 9-1-1 complex) that is recruited onto DNA upon damage. DNA damage also triggers the recruitment of DNA repair proteins at the lesion, including specialized DNA polymerases. In this work, we showed that the 9-1-1 complex can physically interact with DNA polymerase ß in vitro. Functional analysis revealed that the 9-1-1 complex had a stimulatory effect on DNA polymerase ß activity. However, the presence of 9-1-1 complex neither affected DNA polymerase {lambda}, another X family DNA polymerase, nor the two replicative DNA polymerases {alpha} and {delta}. DNA polymerase ß stimulation resulted from an increase in its affinity for the primer–template and the interaction with the 9-1-1 complex stimulated deoxyribonucleotides misincorporation by DNA polymerase ß. In addition, the 9-1-1 complex enhanced DNA strand displacement synthesis by DNA polymerase ß on a 1 nt gap DNA substrate. Our data raise the possibility that the 9-1-1 complex might attract DNA polymerase ß to DNA damage sites, thus connecting directly checkpoints and DNA repair.


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