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B‐ myb proto‐oncogene products interact in vivo with each other via the carboxy‐terminal conserved region
Author(s) -
Kim Taenam,
Jung Haiyoung,
Min Sanghyun,
Kim Kyong-Tai,
Ha Hyunjung
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01375-7
Subject(s) - myb , yeast , in vivo , biology , saccharomyces cerevisiae , oncogene , microbiology and biotechnology , dephosphorylation , biochemistry , genetics , phosphorylation , transcription factor , gene , phosphatase , cell cycle
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.