Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing.
Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing.
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DOI：
10.1210/jcem.84.11.6235
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发表时间：
1999-11
期刊：
影响因子：
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通讯作者：
Caroline A. Rivers;Andrew Levy;Jerry P. Hancock;S. Lightman;Michael E. Norman
中科院分区：
文献类型：
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作者：
Caroline A. Rivers;Andrew Levy;Jerry P. Hancock;S. Lightman;Michael E. Norman
当人类糖皮质激素受体（GR）首次测序时，确定了主要形式（GR α）和次要变体（GR β）。在目前的通信中，我们描述了一种新的变体的糖皮质激素受体（GR γ），其中，作为选择性剪接的结果，三个碱基保留从内含子分离外显子3和4。这三个碱基编码受体的DNA结合结构域中的额外氨基酸（精氨酸）。在此位点插入精氨酸之前已被证明可将GR的转录激活降低至GR α的48%。不同组织的cDNA分析表明，新形式广泛表达在一个相对较高的水平（总GR的3.8%和8.7%之间）。
When the human glucocorticoid receptor (GR) was first sequenced, a predominant form (GRalpha) and a minor variant (GRbeta) were identified. In the present communication, we describe a new variant of the glucocorticoid receptor (GRgamma) in which, as a result of alternative splicing, three bases are retained from the intron separating exons 3 and 4. These three bases code for an additional amino acid (arginine) in the DNA binding domain of the receptor. Insertion of arginine at this site has previously been shown to decrease transcriptional activation by the GR to 48% that of GRalpha. Analysis of cDNA from different tissues shows that the novel form is widely expressed at a relatively high level (between 3.8 and 8.7% of total GR).