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Biochemical and biological activities of Myc oncoproteins are highly dependent upon their association with another basic region helix–loop–helix/leucine zipper (bHLH/LZ) protein, Max. Our previous observation that the DNA-binding/dimerization region of Max is absolutely conserved throughout vertebrate evolution provided the basis for a yeast two-hybrid interaction screen that led to the isolation of theDrosophila Myc (dMyc1) protein. Structural conservation in regions of known functional significance is consistent with the ability of dMyc1 to interact with vertebrate Max, to transactivate gene expression in yeast cells, and to cooperate with activated H-RAS to effect the malignant transformation of primary mammalian cells. The ability ofP -element-mediated ectopic expression ofdmyc1 to reverse a subset of the phenotypic alterations associated with thediminutive mutation suggests thatdiminutive may correspond todmyc1 . This finding, along with the localization ofdmyc1 expression to zones of high proliferative activity in the embryo, implicates dMyc1 as an integral regulator ofDrosophila growth and development.

Drosophila Myc is oncogenic in mammalian cells and plays a role in the diminutive phenotype