Individual repeats of Drosophila Myb can function in transformation by v-Myb

The v-Myb protein binds to specific DNA sequences and can regulate gene expression. The DNA-binding domain of v-Myb contains the second and third of the three highly conserved tandem repeats found in c-Myb. In general, the ability of mutant forms of v-Myb to transform correlates with their ability t...

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Bibliographic Details
Published in:Journal of Virology 1993-12, Vol.67 (12), p.7332-7339
Main Authors: Bin, X, Lipsick, J.S
Format: Article
Language:English
Subjects:
Acetyltransferases
ADN
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Carcinogenesis, carcinogens and anticarcinogens
Cell Transformation, Neoplastic - genetics
Cells, Cultured
CELLULE SANGUINE
CELULAS SANGUINEAS
Chick Embryo
DNA-Binding Proteins - metabolism
Drosophila - genetics
DROSOPHILA MELANOGASTER
Genetic Vectors
GENETICA
GENETIQUE
Hematopoietic Stem Cells
Macrophage-1 Antigen - biosynthesis
Medical sciences
Molecular Sequence Data
Oncogene Proteins v-myb
ONCOVIRUS AVIAIRE
ONCOVIRUS AVIAR
POLLO
POULET
PROTEINAS
PROTEINE
Proteins - genetics
Quail
Recombinant Fusion Proteins - genetics
Repetitive Sequences, Nucleic Acid
Retroviridae - genetics
Retroviridae Proteins, Oncogenic - genetics
Sequence Homology, Amino Acid
Transcriptional Activation
Tumors
VIRUS DE LOS ANIMALES
VIRUS DES ANIMAUX
Viruses
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Description
Summary:The v-Myb protein binds to specific DNA sequences and can regulate gene expression. The DNA-binding domain of v-Myb contains the second and third of the three highly conserved tandem repeats found in c-Myb. In general, the ability of mutant forms of v-Myb to transform correlates with their ability to trans activate transcription. Two mutations within the DNA-binding domain of v-Myb which preserve DNA binding in vitro but fail to trans activate or transform have been described. These results suggested that this highly conserved domain might function in specific protein-protein interactions, as well as in DNA binding. We therefore tested the ability of a related protein domain from Drosophila melanogaster to substitute functionally for the homologous region of v-Myb. We found that either the second or third repeat of Drosophila Myb, but not both, could function in trans-activation and transformation by v-Myb. The hybrid containing both the second and third repeats of Drosophila Myb bound to DNA but failed to trans activate transcription either in the context of v-Myb or as a v-Myb-VP16 fusion protein. These results demonstrate that although the protein-DNA contacts made by the Myb repeats have been conserved during the evolution of animals, the protein-protein interactions have diverged
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.67.12.7332-7339.1993