Functional interaction between the two zinc finger domains of the v-erb A oncoprotein.

B. L. Hall, B. G. Bonde, C. Judelson, M. L. Privalsky

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The v-erb A oncogene of avian erythroblastosis virus is a mutated and virally transduced copy of a host cell gene encoding a thyroid hormone receptor. The protein expressed by the v-erb A oncogene binds to DNA and acts as a dominant negative inhibitor of both the thyroid hormone receptor and the closely related retinoic acid receptor. The v-erb A protein has sustained two amino acid alterations within its DNA-binding domain relative to that of c-erb A, one of which, at serine 61, is known to be important for v-erb A function in the neoplastic cell. We report here that the second alteration, at threonine 78, also plays an important, although more indirect, role: alteration of the sequence at threonine 78 such that it resembles that of c-erb A can act as an intragenic suppressor and can partially restore function to a v-erb A protein rendered defective due to a mutation at position 61. Threonine 78 lies within the D-box of the v-erb A protein, a region thought to mediate receptor-receptor dimerizations, and is not in physical proximity to the serine at position 61. It therefore appears that an indirect interaction occurs between these two sites and that this interaction is crucial for v-erb A function.

Original languageEnglish (US)
Pages (from-to)207-216
Number of pages10
JournalCell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
Volume3
Issue number4
StatePublished - Apr 1992

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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