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J Biol Chem, Vol. 273, Issue 45, 29794-29800, November 6, 1998

MM-1, a Novel c-Myc-associating Protein That Represses Transcriptional Activity of c-Myc

Katsuhiro MoriDagger , Yuichi MaedaDagger , Hirotake KitauraDagger , Takahiro TairaDagger , Sanae M. M. Iguchi-Ariga§, and Hiroyoshi ArigaDagger

From the Dagger  Graduate School of Pharmaceutical Sciences and § College of Medical Technology, Hokkaido University, Kita-ku, Sapporo 060, Japan

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.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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