Abstract
ISHII, S., NOMURA, T., KANEI-ISHII, C., NAKAGOSHI, H., SUDO, T. and SAWAZAKI, T. Transcriptional Control by myb Oncogene Product. Tohoku J. Exp. Med., 1992, 162 (2), 189-194-Structure and function of two domains of c-Myb were analyzed. We show that a leucine zipper structure is a component of the negative regulatory domain, because its disruption markedly increases both the transactivating and transforming capacities of c-Myb. Our results suggest that an inhibitor which suppresses transactivation binds to c-Myb through the leucine zipper, and that c-Myb can be oncogenically activated by mis-sense mutation. We also proposed a model, the “tryptophan cluster”, for the structure of the Myb DNA-binding domain, in which the three tryptophans form a cluster in the hydrophobic core in each repeat. The results of NMR analysis of repeat 3 revealed that the conserved tryptophans play a key role to make the hydrophobic core. -sequence-specific DNA-binding protein ; negative regulatory domain; leucine zipper; NMR
