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.
|Original language||English (US)|
|Number of pages||11|
|Journal||Journal of Virology|
|State||Published - 1988|
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