Mapping of functional domains within the v-erb A oncogene protein: the remnants of the hormone binding domain play multiple, vital roles in protein action.
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 demonstrates 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 distinguishable from one another, and encompass sequences projecting beyond the zinc-finger motifs themselves. Although unable to bind T3 thyroid hormone, the remnants of the hormone binding domain continue to play unanticipated essential roles in v-erb A protein function.
Boucher
P
P
Department of Microbiology, University of California, Davis 95616.
Privalsky
M L
ML
D002467:Cell Nucleus / Q000378:metabolism*; D002472:Cell Transformation, Viral / Q000235:genetics*; D002874:Chromosome Mapping; D004247:DNA / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D015750:Genes, gag / Q000235:genetics*; D009154:Mutation / Q000235:genetics*; D011518:Proto-Oncogene Proteins / Q000235:genetics* / Q000378:metabolism; D011988:Receptors, Thyroid Hormone; D013963:Thyroid Hormones / Q000378:metabolism; D014158:Transcription, Genetic
D011518:Proto-Oncogene Proteins; D011988:Receptors, Thyroid Hormone; D013963:Thyroid Hormones; D004247:DNA