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首页> 外文期刊>Molecular and Cellular Biology >A 36-kilodalton cellular transcription factor mediates an indirect interaction of human T-cell leukemia/lymphoma virus type I TAX1 with a responsive element in the viral long terminal repeat.
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A 36-kilodalton cellular transcription factor mediates an indirect interaction of human T-cell leukemia/lymphoma virus type I TAX1 with a responsive element in the viral long terminal repeat.

机译:36千达尔顿细胞转录因子介导人T细胞白血病/淋巴瘤病毒I TAX1与病毒长末端重复序列中的应答元件间接相互作用。

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The human T-cell leukemia/lymphoma virus type I (HTLV-I) trans activator, TAX1, interacts indirectly with a TAX1-responsive element, TRE-2, located at positions -117 to -163 in the viral long terminal repeat. This report describes the characterization of a 36-kilodalton (kDa) protein identified in HeLa nuclear extract which mediates the interaction of TAX1 with TRE-2. Purification of the protein was achieved by zinc chelate chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The renatured 36-kDa protein bound specifically to a TRE-2 oligonucleotide but not to nonfunctional base substitution mutant probes in a gel retardation assay. Renatured proteins of differing molecular weights were unable to form this complex. In addition, the 36-kDa protein specifically activated transcription from the HTLV-I promoter in vitro. Purified TAX1 protein formed a complex with the TRE-2 oligonucleotide in the presence of the 36-kDa protein, suggesting that indirect interaction of TAX1 with the viral long terminal repeat may be one of the mechanisms by which HTLV-I transcription is regulated.
机译:I型人T细胞白血病/淋巴瘤病毒(HTLV-1)反式激活剂TAX1与TAX-1反应元件TRE-2间接相互作用,该元件位于病毒长末端重复序列中的-117至-163位。该报告描述了在HeLa核提取物中鉴定出的36千达尔顿(kDa)蛋白的特征,该蛋白介导TAX1与TRE-2的相互作用。通过螯合锌层析和制备型十二烷基硫酸钠-聚丙烯酰胺凝胶电泳实现蛋白质的纯化。在凝胶阻滞分析中,经过变性的36 kDa蛋白与TRE-2寡核苷酸特异性结合,但与非功能性碱基取代突变探针没有特异性结合。分子量不同的变性蛋白质无法形成这种复合物。另外,该36-kDa蛋白在体外特异性激活了HTLV-1启动子的转录。纯化的TAX1蛋白在36 kDa蛋白存在下与TRE-2寡核苷酸形成复合物,这表明TAX1与病毒长末端重复序列的间接相互作用可能是HTLV-1转录调控的机制之一。

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