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	J. Biol. Chem. Nov (1998); 273(45):29794-800
MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc.
Mori K, Maeda Y, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H
Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo 060, Japan.
Abstract: We have isolated the cDNA encoding a novel c-Myc-binding protein, MM-1, by the yeast two-hybrid screening of a human HeLa cell cDNA library. The protein deduced from the cDNA comprises 167 amino acids and was localized in the nucleus of introduced COS-I cells. The MM-1 mRNA was highly expressed in human pancreas and skeletal muscle and moderately in other tissues. As for the c-Myc binding, glutathione S-transferase MM-1 expressed in Escherichia coli bound in vitro to c-Myc translated in reticulocyte lysate, and almost whole, the MM-1 molecule was necessary for the binding in the yeast two-hybrid system. The mammalian two-hybrid assays in hamster CHO cells revealed that MM-1 interacts in vivo with the N-terminal domain covering the myc box 2, a transcription-activating domain, of c-Myc. Furthermore, MM-1 repressed the activation of E-box-dependent transcription by c-Myc.
[PUBMED: 9792694]