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Originally published In Press as doi:10.1074/jbc.M006990200 on September 12, 2000

J. Biol. Chem., Vol. 275, Issue 48, 37469-37473, December 1, 2000
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p53 and c-Jun Functionally Synergize in the Regulation of the DNA Repair Gene hMSH2 in Response to UV*

Stefan J. SchererDagger §, Sandra M. MaierDagger , Markus SeifertDagger , Rainer G. Hanselmann, Klaus D. ZangDagger , Hans K. Müller-Hermelink||, Peter Angel**, Cornelius WelterDagger , and Manfred Schartl§Dagger Dagger

From the Dagger  Department of Human Genetics, University of Saarland, Geb. 68, D-66421 Homburg/Saar, the § Department of Physiological Chemistry I, Biocenter, University of Würzburg, Am Hubland, 97074 Würzburg, the  Department of Experimental Physics, University of Saarland, Geb. 22, 68111 Saarbrücken, the || Department of Pathology, University of Würzburg, Josef Schneider Straße 2, 97080 Würzburg, and the ** Division of Signal Transduction and Growth Control, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

The tumor suppresser protein p53 is critical for guarding the genome from incorporation of damaged DNA (Lane, D. P. (1992) Nature 358, 15-16). A relevant stress that activates p53 function is UV light (Noda, A., Toma-Aiba, Y., and Fujiwara, Y. (2000) Oncogene 19, 21-31). Another well known component of the mammalian UV response is the transcription factor c-Jun (Angel, P., and Karin, M. (1991) Biochim. Biophys. Acta 1072, 129-157). We show here that upon UV irradiation p53 activates transcription of the human mismatch repair gene MSH2. Interestingly, this up-regulation critically depends on functional interaction with c-Jun. Hence, the synergistic interaction of a proto-oncogene with a tumor suppresser gene is required for the regulation of the mammalian stress response through activation of expression of MSH2.

* This work was supported by a fellowship of the Interdisziplinäres Zentrum für Klinische Forschung Würzburg (to S. S.) and grants supplied by the Deutsche Forschungsgemeinschaft through SFB 465 and Fonds der Chemischen Industrie (to M. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger To whom correspondence should be addressed: Dept. of Physiological Chemistry I, Biocenter of the University of Wuerzburg, Am Hubland, D-97074 Wuerzburg, Germany. Tel.: 931-888-4149; Fax: 931888-4150; E-mail: phch1@biozentrum.uni-wuerzburg.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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