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Nucleic Acids Research, 2002, Vol. 30, No. 11 2340-2348
© 2002 Oxford University Press

Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277

Jiri Buzek, Leena Latonen, Sari Kurki, Karita Peltonen and Marikki Laiho*

Department of Virology, Haartman Institute, and Molecular Cancer Biology Program, Biomedicum Helsinki, University of Helsinki and Helsinki University Central Hospital Laboratory Diagnostics, PO Box 63, FIN-00014 Helsinki, Finland

Using a bio-oligo pull-down DNA-binding assay we investigated the binding capacity of endogenous, DNA damage-induced p53 in human diploid fibroblasts to several p53-responsive elements (REs) present in p53-regulated genes. During the course of p53 accumulation, we observed a decrease in p53 binding to the GADD45 but not to the p21WAF1/CIP1 RE. Using mutated GADD45 sequences we show that this change is dependent on the presence of cytosines at position 3 in RE pentamers and on the p53 redox state. Site-directed mutagenesis experiments demonstrated that Cys277 (a residue directly contacting base 3 in a RE pentamer) is critical for differential regulation of GADD45 in DNA-damaged cells. These data represent a novel mechanism for differential affinity of p53 to distinct REs.

* To whom correspondence should be addressed at: Haartman Institute, Department of Virology, University of Helsinki, PO Box 63, FIN-00014 Helsinki, Finland. Tel: +358 9 1912 5540; Fax: +358 9 1912 5554; Email: marikki.laiho{at}helsinki.fi Present address:Jiri Buzek, Institute of Biophysics, Academy of Sciences of the Czech Republic, Kralovopolska 135, 612 65 Brno, Czech Republic


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