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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Interactions between human cyclin T, Tat, and the transactivation response element (TAN) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T
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Interactions between human cyclin T, Tat, and the transactivation response element (TAN) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

机译：人细胞周期蛋白T，Tat和反式激活反应元件（TAN）之间的相互作用被小鼠细胞周期蛋白T中的半胱氨酸取代为酪氨酸而破坏

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摘要

The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of viral transcription. Human cyclin T supports these interactions between Tat and TAR. In this study, we report the sequence of mouse cyclin T and identify the residues from positions 1 to 281 in human cyclin T that bind to Tat and TAR. Mouse cyclin T binds to Tat weakly and is unable to facilitate interactions between Tat and TAR. Reciprocal exchanges of the cysteine and tyrosine at position 261 in human and mouse cyclin T proteins also render human cyclin T inactive and mouse cyclin T active. These findings reveal the molecular basis for the restriction of Tat transactivation in rodent cells.
机译：来自HIV的转录反式激活因子Tat与反式激活应答元件（TAR）RNA结合，从而提高了病毒转录的延伸率。人类细胞周期蛋白T支持Tat和TAR之间的这些相互作用。在这项研究中，我们报告了小鼠细胞周期蛋白T的序列，并鉴定了人细胞周期蛋白T中与Tat和TAR结合的1至281位的残基。小鼠细胞周期蛋白T与Tat的结合较弱，无法促进Tat与TAR之间的相互作用。人和小鼠细胞周期蛋白T蛋白中261位的半胱氨酸和酪氨酸的相互交换也使人细胞周期蛋白T失活而小鼠细胞周期蛋白T活跃。这些发现揭示了限制啮齿动物细胞中Tat反式激活的分子基础。

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