Transactivation and transformation by Myb are negatively regulated by a leucine-zipper structure.
The negative regulatory domain of the c-myb protooncogene product (c-Myb) normally represses transcriptional activation by c-Myb. We show here 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. We also demonstrate that this leucine-zipper structure can interact with cellular proteins. Our results suggest that an inhibitor that suppresses transactivation binds to c-Myb through the leucine zipper and that c-Myb can be oncogenically activated by missense mutation.
Kanei-Ishii
C
C
Tsukuba Life Science Center, Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.
MacMillan
E M
EM
Nomura
T
T
Sarai
A
A
Ramsay
R G
RG
Aimoto
S
S
Ishii
S
S
Gonda
T J
TJ
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000502:physiology*; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D066298:In Vitro Techniques; D016350:Leucine Zippers; D046911:Macromolecular Substances; D051379:Mice; D008969:Molecular Sequence Data; D011485:Protein Binding; D011518:Proto-Oncogene Proteins / Q000502:physiology*; D020598:Proto-Oncogene Proteins c-myb; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D011518:Proto-Oncogene Proteins; D020598:Proto-Oncogene Proteins c-myb