The Steroid/Thyroid Hormone Receptor Family and Gene Regulation

The Steroid/Thyroid Hormone Receptor Family and Gene Regulation
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类固醇/甲状腺激素受体家族和基因调控

DOI:
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发表时间:
1998
期刊:
Birkhäuser Congress Reports Life Sciences
影响因子:
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通讯作者:
J. Gustafsson
J. Gustafsson
中科院分区:
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文献类型:
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作者:
J. Carlstedt;H. Eriksson;J. Gustafsson

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由细胞原癌基因c-erbA和其病毒同源物verbA编码的erbA蛋白质在它们的DNA结合区域以及其他结构域中不同。我们研究了这些蛋白质在转录调控和与甲状腺激素反应元件(TREs)结合方面可能存在的差异。结果表明,在鸡成红细胞P7 Sgag-v-erbA组成型抑制带3和碳酸酐酶的基因的表达,而正常的甲状腺激素受体抑制表达的配体的情况下,并诱导转录后结合的激素。在一个直接的测试结合到TREs在大鼠生长激素基因的c-erbA蛋白结合具有高亲和力,而病毒蛋白表现出没有结合在所有。实验表明,这两种蛋白质可以识别成红细胞中相同的调控元件,但对转录具有不同的影响,并且其他TREs仅与其中一种蛋白质结合,这表明病毒蛋白质一级结构中的突变改变了其特异性。
The erbA proteins encoded by the cellular proto-oncogene c-erbA and its viral homologue verbA differ in their DNA binding region as well as in other domains. We have investigated the possible differences in regulation of transcription and the binding to thyroid hormone responsive elements (TREs) by these proteins. The results show that in chicken erythroblasts P7Sgag-v-erbA constitutively represses expression of the genes for band 3 and carbonic anhydrase, whereas the normal thyroid hormone receptor represses expression in the absence of ligand and induces transcription upon binding of hormone. In a direct test of binding to TREs in the rat growth hormone gene the c-erbA protein bound with high affinity, whereas the viral ptotein exhibited no binding at all. The experiments demonstrate that the two proteins can recognize the same regulatory elements in erythroblasts but with distinct effects on transcription, and that other TREs bind to only one of the proteins, suggesting that mutations in the primary structure of the viral protein has altered its specificity.