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MBC in Press, published online ahead of print May 7, 2008
Mol. Biol. Cell 10.1091/mbc.E07-11-1167

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Submitted on November 20, 2007
Revised on March 14, 2008
Accepted on April 24, 2008

Rad54B Targeting to DNA Double-Strand Break Repair Sites Requires Complex Formation with S100A11

Ulrike Murzik,* Peter Hemmerich,{dagger} Stefanie Weidtkamp-Peters,{dagger}{ddagger} Tobias Ulbricht,{dagger} Wendy Bussen,{sect}|| Julia Hentschel,* Ferdinand von Eggeling,* and Christian Melle*

*Core Unit Chip Application (CUCA), Institute of Human Genetics and Anthropology, Medical Faculty, Friedrich-Schiller-University, 07740 Jena, Germany; {dagger}Department of Molecular Biology, Fritz Lipmann Institut (FLI) - Leibniz Institute for Age Research, 07708 Jena, Germany; {sect}Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06515

Monitoring Editor: M. Bishr Omary

S100A11 is involved in a variety of intracellular activities such as growth regulation and differentiation. To gain more insight into the physiological role of endogenously expressed S100A11 we used a proteomic approach to detect and identify interacting proteins in vivo. Hereby, we were able to detect a specific interaction between S100A11 and Rad54B which could be confirmed under in vivo conditions. Rad54B, a DNA-dependent ATPase, is described to be involved in recombinational repair of DNA damage, inluding DNA double-strand breaks (DSBs). Treatment with bleomycin, which induces DSBs, revealed an increase in the degree of colocalization between S100A11 and Rad54B. Furthermore, S100A11/Rad54B foci are spatialy associated with sites of DNA double-strand break repair. Furthermore, while the expression of p21WAF1/CIP1 was increased in parallel with DNA damage, its protein level was drastically down-regulated in damaged cells after S100A11 knock-down. Down-regulation of S100A11 by RNA interference also abolished Rad54B targeting to DSBs. Additionally, S100A11 down-regulated HaCaT cells showed a restricted proliferation capacity and an increase of the apoptotic cell fraction. These observations suggest that S100A11 targets Rad54B to sites of DNA double-strand break repair sites and identify a novel function for S100A11 in p21-based regulation of cell cycle.

Address correspondence to:

present addresses: {ddagger}Lehrstuhl für Molekulare Physikalische Chemie, Institut für Physikalische Chemie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany; ||Department of Radiation Oncology, Washington University School of Medicine, St. Louis, MO 63108. Christian Melle (christian.melle{at}mti.uni-jena.de)






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