The avian erythroblastosis virus erbA oncogene encodes a DNA-binding protein exhibiting distinct nuclear and cytoplasmic subcellular localizations.
The protein product of the v-erbA oncogene of avian erythroblastosis virus was analyzed by use of site-specific antisera. The v-erbA protein was found to exist in distinct nuclear and cytoplasmic forms. Both nuclear and cytoplasmic species of the v-erbA protein were capable of binding to DNA, a property predicted based on the structural relatedness the v-erbA polypeptide shares with the thyroid and steroid hormone receptors. A mutation within the v-erbA coding region which inhibited DNA binding and nuclear localization also inhibited the ability of the v-erbA protein to potentiate erythroid transformation, consistent with a model of the v-erbA protein as a transcriptional regulator.
Boucher
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P
Department of Biochemistry/Biophysics, University of California, Davis 95616.
Koning
A
A
Privalsky
M L
ML
D001355:Alpharetrovirus / Q000235:genetics*; D000818:Animals; D001354:Avian Leukosis Virus / Q000235:genetics*; D002467:Cell Nucleus / Q000032:analysis; D002642:Chick Embryo; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000032:analysis; D004268:DNA-Binding Proteins / Q000032:analysis / Q000235:genetics*; D005347:Fibroblasts; D005455:Fluorescent Antibody Technique; D005814:Genes, Viral; D007118:Immunoassay; D009154:Mutation; D009857:Oncogenes; D012191:Retroviridae Proteins / Q000032:analysis / Q000235:genetics*
D004268:DNA-Binding Proteins; D012191:Retroviridae Proteins; C040520:avian retrovirus proteins