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The highly conserved amino‐terminal region of the protein encoded by the v‐myb oncogene functions as a DNA‐binding domain.
Author(s) -
Klempnauer K. H.,
Sippel A. E.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02565.x
Subject(s) - myb , biology , chromatin , microbiology and biotechnology , dna , dna binding protein , genetics , gene , transcription factor
The retroviral oncogene v‐myb encodes a 45,000 Mr nuclear protein (p45v‐myb) that is predominantly associated with the chromatin of transformed cells. It has previously been shown that p45v‐myb, when released from chromatin by salt‐treatment, binds to DNA. To analyse the biochemical properties of p45v‐myb in more detail we have expressed the v‐myb coding region in Escherichia coli. Our results demonstrate that bacterially expressed myb protein has an intrinsic DNA‐binding activity. Using two alternative strategies, (i) inhibition of DNA‐binding by monoclonal antibodies and (ii) analysis of DNA‐binding activities of partially deleted forms of the bacterial myb protein, we show that the DNA‐binding domain is located in the amino‐terminal region of the v‐myb protein. This region has been highly conserved between myb genes of different species. Our results are therefore consistent with the hypothesis that DNA‐binding is an important aspect of myb protein function.