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一种36千道尔顿的细胞转录因子介导了人类I型T细胞白血病/淋巴瘤病毒TAX1与病毒长末端重复序列中一个反应元件的间接相互作用。

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.

作者信息

Marriott S J, Lindholm P F, Brown K M, Gitlin S D, Duvall J F, Radonovich M F, Brady J N

机构信息

Laboratory of Molecular Virology, National Cancer Institute, Bethesda, Maryland 20892.

出版信息

Mol Cell Biol. 1990 Aug;10(8):4192-201. doi: 10.1128/mcb.10.8.4192-4201.1990.

DOI:10.1128/mcb.10.8.4192-4201.1990
PMID:2370863
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC360951/
Abstract

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.

摘要

人类I型T细胞白血病/淋巴瘤病毒（HTLV-I）反式激活因子TAX1与位于病毒长末端重复序列中-117至-163位的TAX1反应元件TRE-2间接相互作用。本报告描述了在HeLa细胞核提取物中鉴定出的一种36千道尔顿（kDa）蛋白质的特性，该蛋白质介导TAX1与TRE-2的相互作用。通过锌螯合层析和制备性十二烷基硫酸钠-聚丙烯酰胺凝胶电泳实现了该蛋白质的纯化。在凝胶阻滞试验中，复性的36-kDa蛋白质特异性结合TRE-2寡核苷酸，但不结合无功能的碱基替代突变探针。不同分子量的复性蛋白质无法形成这种复合物。此外，36-kDa蛋白质在体外特异性激活HTLV-I启动子的转录。在36-kDa蛋白质存在的情况下，纯化的TAX1蛋白质与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-I转录调控的机制之一。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/efec85aded5b/molcellb00044-0352-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/f639382ee89c/molcellb00044-0348-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/506b332c9dbf/molcellb00044-0348-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/42138ab5f715/molcellb00044-0349-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/9a5e72bca288/molcellb00044-0350-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/f3aa3bdd30cc/molcellb00044-0351-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/efec85aded5b/molcellb00044-0352-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/f639382ee89c/molcellb00044-0348-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/506b332c9dbf/molcellb00044-0348-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/42138ab5f715/molcellb00044-0349-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/9a5e72bca288/molcellb00044-0350-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/f3aa3bdd30cc/molcellb00044-0351-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/782b/360951/efec85aded5b/molcellb00044-0352-a.jpg

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