未结合配体的甲状腺激素受体α可靶向TATA结合蛋白以进行转录抑制。
Unliganded thyroid hormone receptor alpha can target TATA-binding protein for transcriptional repression.
作者信息
Fondell J D, Brunel F, Hisatake K, Roeder R G
机构信息
Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, New York 10021, USA.
出版信息
Mol Cell Biol. 1996 Jan;16(1):281-7. doi: 10.1128/MCB.16.1.281.
Abstract
Unliganded human thyroid hormone receptor alpha (hTR alpha) can repress transcription by inhibiting the formation of a functional preinitiation complex (PIC) on promoters bearing thyroid hormone receptor (TR)-binding elements. Here we demonstrate that hTR alpha directly contacts the TATA-binding protein (TBP) and that preincubation of hTR alpha with TBP completely alleviates TR-mediated repression in vitro. Using stepwise preassembled PICs, we show that hTR alpha targets either the TBP/TFIIA or the TBP/TFIIA/TFIIB steps of PIC assembly for repression. We also show that the repression domain of hTR alpha maps to the C-terminal ligand-binding region and that direct TR-TBP interactions can be inhibited by thyroid hormone. Together, these results suggest a model in which unliganded hTR alpha contacts promoter-bound TBP and interferes with later steps in the initiation of transcription.
摘要
未结合配体的人甲状腺激素受体α（hTRα）可通过抑制在带有甲状腺激素受体（TR）结合元件的启动子上形成功能性起始前复合物（PIC）来抑制转录。在此我们证明，hTRα直接与TATA结合蛋白（TBP）接触，并且hTRα与TBP的预孵育在体外完全减轻了TR介导的抑制作用。使用逐步预组装的PIC，我们表明hTRα靶向PIC组装的TBP/TFIIA或TBP/TFIIA/TFIIB步骤以进行抑制。我们还表明，hTRα的抑制结构域定位于C末端配体结合区域，并且甲状腺激素可抑制TR与TBP的直接相互作用。总之，这些结果提示了一种模型，其中未结合配体的hTRα与启动子结合的TBP接触并干扰转录起始的后续步骤。
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