Transcriptional Control by myb Oncogene Product

Shunsuke Ishii, Teruaki Nomura, Chie Kanei-ishii, Hideki Nakagoshi, Tatsuhiko Sudo, Tetsuya Sawazaki

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)189-194
Number of pages6
JournalTohoku Journal of Experimental Medicine
Issue number2
Publication statusPublished - 1992
Externally publishedYes


  • NMR
  • leucine zipper
  • negative regulatory domain
  • sequence-specific DNA-binding protein

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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