B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region.
Using the yeast two-hybrid assay and in vivo binding assay, we investigated whether B-myb oncogene products (B-myb) can associate with each other. Specificity tests of the yeast two-hybrid system showed a self-association of B-myb proteins in yeast. Cotransfection experiments demonstrated that B-myb proteins form a complex in vivo. Deletion analysis revealed that this binding was sufficiently mediated by the carboxy-terminal conserved region of B-myb. In addition, the B-myb self-association is directly dependent on the amount of expressed B-myb in cells and slightly increased by the dephosphorylation state. These results suggested that B-myb could form a complex and influence its transcriptional activity.
Kim
T
T
Department of Biochemistry and Division of Life Sciences, Chungbuk National University, Cheongju, South Korea.
Jung
H
H
Min
S
S
Kim
K T
KT
Ha
H
H
D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D006801:Humans; D008957:Models, Genetic; D016296:Mutagenesis; D010766:Phosphorylation; D011485:Protein Binding; D000090063:Proto-Oncogene Mas; D020598:Proto-Oncogene Proteins c-myb / Q000378:metabolism*; D014162:Transfection; D020798:Two-Hybrid System Techniques
D018076:DNA, Complementary; D004268:DNA-Binding Proteins; C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D020598:Proto-Oncogene Proteins c-myb