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MDM2 is a 90 kDa nucleo-phosphoprotein that binds p53 and other proteinscontributing to its oncogenic properties. Its structure includes an amino proximalp53 binding site, a central acidic domain and a carboxy region which incorporatesZinc and Ring Finger domains suggestive of nucleic acid binding or transcriptionfactor function. It has previously been reported that a bacculovirus expressedMDM2 protein binds RNA in a sequence-specific manner through the Ring Finger domain,however, its ability to bind DNA has yet to be examined. We report here that abacterially expressed human MDM2 protein binds both DNA as well as the previouslydefined RNA consensus sequence. DNA binding appears selective and involves thecarboxy-terminal domain of the molecule. RNA binding is inhibited by an MDM2 specificantibody, which recognises an epitope within the carboxy region of the protein.Selection cloning and sequence analysis of MDM2 DNA binding sequences, unlikeRNA binding sequences, revealed no obvious DNA binding consensus sequence, butpreferential binding to oligopurine:pyrimidine-rich stretches. Our results suggestthat the observed preferential DNA binding may occur through the Zinc Finger orin a charge-charge interaction through the Ring Finger, thereby implying potentiallydifferent mechanisms for DNA and RNA MDM2 binding.

Recombinant human MDM2 oncoprotein shows sequence composition selectivity for binding to both RNA and DNA