Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product.
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Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product. / Sap, J; Muñoz, A; Schmitt, J; Stunnenberg, H; Vennström, B.
In: Nature, Vol. 340, No. 6230, 1989, p. 242-4.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product.
AU - Sap, J
AU - Muñoz, A
AU - Schmitt, J
AU - Stunnenberg, H
AU - Vennström, B
N1 - Keywords: Base Sequence; Gene Expression Regulation; Immunosorbent Techniques; Moloney murine leukemia virus; Oncogene Proteins v-erbA; Oncogenes; Plasmids; Promoter Regions (Genetics); Receptors, Thyroid Hormone; Repetitive Sequences, Nucleic Acid; Retroviridae Proteins; Sequence Homology, Nucleic Acid; Simplexvirus; Thyroid Hormones; Transcription, Genetic; Transfection; Triiodothyronine
PY - 1989
Y1 - 1989
N2 - Several recent observations, such as the identification of the cellular homologue of the v-erb-A oncogene as a thyroid-hormone receptor, have strongly implicated nuclear oncogenes in transcriptional control mechanisms. The v-erb-A oncogene blocks the differentiation of erythroid cells, and changes the growth requirements of fibroblasts and erythroblasts. Mutations in v-erb-A protein have led to the loss of its affinity for thyroid hormones but do not affect its DNA-binding ability, a property required for biological activity. We report here the identification of a novel thyroid-hormone response element (TRE) in the long terminal repeat of Moloney murine leukaemia virus that binds the c-erb-A-alpha protein. The v-erb-A protein abolishes the responsiveness of this TRE to thyroid hormone, although it has a lower affinity than the normal receptor for the TRE. The data indicate that overexpressed v-erb-A protein negatively interferes with normal transcriptional-control mechanisms, and that amino-acid substitutions have altered its DNA-binding properties.
AB - Several recent observations, such as the identification of the cellular homologue of the v-erb-A oncogene as a thyroid-hormone receptor, have strongly implicated nuclear oncogenes in transcriptional control mechanisms. The v-erb-A oncogene blocks the differentiation of erythroid cells, and changes the growth requirements of fibroblasts and erythroblasts. Mutations in v-erb-A protein have led to the loss of its affinity for thyroid hormones but do not affect its DNA-binding ability, a property required for biological activity. We report here the identification of a novel thyroid-hormone response element (TRE) in the long terminal repeat of Moloney murine leukaemia virus that binds the c-erb-A-alpha protein. The v-erb-A protein abolishes the responsiveness of this TRE to thyroid hormone, although it has a lower affinity than the normal receptor for the TRE. The data indicate that overexpressed v-erb-A protein negatively interferes with normal transcriptional-control mechanisms, and that amino-acid substitutions have altered its DNA-binding properties.
U2 - 10.1038/340242a0
DO - 10.1038/340242a0
M3 - Journal article
C2 - 2569164
VL - 340
SP - 242
EP - 244
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6230
ER -
ID: 5070200