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Nucleic Acids Research, 1988, Vol. 16, No. 23 11075-11089
© 1988


MOLECULAR BIOLOGY

Isolation of human cDNA clones of myb-related genes, A-myb and B-myb

Nobuo Nomura, Masayoshi Takahashi1, Minami Matsui, Shunsuke Ishii2, Takayasu Date3, Shigemi Sasamoto and Ryotaro Ishizaki

Molecular Oncology Laboratory, Nippon Veterinary and Zootechnical College Sakuragi, 1-10-19 Uenosakuragi, Taito-ku, Tokyo 110, Japan 1Institute of Applied Microbiology, University of Tokyo Bunkyo-ku, Tokyo 113, Japan 2Laboratory of Physical and Chemical Research RIKEN, 3-1-1 Koya-dai, Tsukuba, Ibaraki 305, Japan 3Department of Biochemistry, Kanazawa Medical University Uchinada, Ishikawa 920-02, Japan

Received September 15, 1988. Revised November 8, 1988. Accepted November 8, 1988.

cDNA clones of the myb-related genes A-myb and B-myb were obtained by screening human cDNA libraries. The predicted open reading frame of B-myb could encode a protein of 700 amino acid residues. Although the C-terminal end has not been cloned yet, an almost entire coding region of A-myb which is 745 amino acid long, was determined. The A-myb and B-myb proteins are highly homologous with the myb protein in three regions. Domain I, which is 161 amino acid long, is well conserved in the myb gene family. The homology between human-myb and A-myb in domain I is 90% at the amino acid level. Domain II, which is about 85 amino acid long, is less well conserved. Although it is a short stretch, domain III is found in the C-terminal region. The mRNAS of A-myb and B-myb were 5.0 and 2.6kb, respectively. The mRNA expression pattern of the myb gene family in various tumors is presented.


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