• 1 September 1990
    • journal article
    • research article
    • Vol. 5  (9) , 1303-1311
Abstract
The v-erb A oncogene represents a virally-transduced variant of a thyroid hormone receptor. Biochemical characterization of a series of mutant v-erb A proteins demonstrations that nuclear localization and DNA binding are both necessary for v-erb A function in the neoplastic cell and are mediated by multiple, overlapping domains within the v-erb A polypeptide. Domains of the v-erb A protein necessary for sequence-specific and sequence-independent DNA binding are distinguished from one another, and encompass sequences projecting beyond the zinc-finger motifs themselves. Although unable to bind T3 thtroid hormone, the remnants of the hormone binding domain continue to play unanticipated essential roles in v-erb protein function.

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