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Drosophila and vertebrate myb proteins share two conserved regions, one of which functions as a DNA‐binding domain.
Author(s) -
Peters C. W.,
Sippel A. E.,
Vingron M.,
Klempnauer K. H.
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.tb02616.x
Subject(s) - biology , vertebrate , myb , drosophila (subgenus) , dna binding protein , genetics , conserved sequence , evolutionary biology , dna , drosophilidae , drosophila melanogaster , microbiology and biotechnology , computational biology , transcription factor , base sequence , gene
We report the nucleotide sequence of a cDNA clone of the Drosophila melanogaster homologue of c‐myb, a member of the class of vertebrate transforming genes encoding nuclear proteins. We predict the mol. wt of the Drosophila myb (D‐myb) protein to be 74,000. The D‐myb protein contains two clusters of sequences homologous to vertebrate myb proteins, surrounded by sequences lacking homology. These results extend previous evidence for the existence of a D. melanogaster homologue of c‐myb and identify two highly conserved and therefore presumably functionally important domains of c‐myb proteins. DNA‐binding experiments indicate that the NH2‐proximal of the two homology regions functions as a DNA‐binding domain. Based on the absence of the COOH‐proximal homology region in truncated oncogenic derivatives of c‐myb it is likely that this homology region encodes a function whose loss is involved in activating the oncogenic potential of c‐myb.