Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50
Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50
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DOI：
10.1126/science.285.5433.1576
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发表时间：
1999-09-03
期刊：
影响因子：
56.9
通讯作者：
Manley, JL
中科院分区：
文献类型：
--
作者：
Kleiman, FE;Manley, JL
信使RNA前体的多聚腺苷酸化需要一个复杂的蛋白质机制，该机制与更复杂的转录装置紧密结合。在这里，一个多聚腺苷化因子，CstF-50(切割刺激因子)，被证明在体外和在完整的细胞中与一个以前未知功能的核蛋白，BRCA1相关环域蛋白(BARD1)相互作用。BARD1-CstF-50相互作用在体外可抑制多聚腺苷酸化。BARD1和CstF-50一样，也与RNA聚合酶II相互作用。这些结果表明，BARD1介导的抑制多聚腺苷基化可能阻止转录过程中不适当的RNA加工，可能是在DNA修复部位，它们揭示了多种核事件的意外整合。
Polyadenylation of messenger RNA precursors requires a complex protein machinery that is closely integrated with the even more complex transcriptional apparatus. Here a polyadenylation factor, CstF-50 (cleavage stimulation factor), is shown to interact in vitro and in intact cells with a nuclear protein of previously unknown function, BRCA1-associated RING domain protein (BARD1). The BARD1-CstF-50 interaction inhibits polyadenylation in vitro. BARD1, like CstF-50, also interacts with RNA polymerase II. These results indicate that BARD1-mediated inhibition of polyadenylation may prevent inappropriate RNA processing during transcription, perhaps at sites of DNA repair, and they reveal an unanticipated integration of diverse nuclear events.