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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II
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An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II

机译：肌动蛋白-核糖蛋白相互作用参与RNA聚合酶II的转录

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摘要

To determine the function of actin in the cell nucleus, we sought to identify nuclear actin-binding proteins in the dipteran Chironomus tentans using DNase I-affinity chromatography. We identified the RNA-binding protein hrp65 as an actin-binding protein and showed that the C-terminal sequence of the hrp65-2 isoform is able to interact directly with actin in vitro. In vivo crosslinking and coimmunoprecipitation experiments indicated that hrp65 and actin are also associated in the living cell. Moreover, in vivo administration of a competing peptide corresponding to the C-terminal sequence of hrp65-2 disrupted the actin-hrp65-2 interaction and caused a specific and drastic reduction of transcription as judged by puff regression and diminished bromo-UTP incorporation. Our results indicate that an actin-based mechanism is implicated in the transcription of most if not all RNA polymerase II genes and suggest that an actin-hrp65-2 interaction is required to maintain the normal transcriptional activity of the cell. Furthermore, immunoelectron microscopy experiments and nuclear run-on assays suggest that the actin-hrp65-2 complex plays a role in transcription elongation. [References: 36]
机译：为了确定肌动蛋白在细胞核中的功能，我们试图使用DNase I亲和色谱法来鉴定二萜Chironomus tentans中的核肌动蛋白结合蛋白。我们确定RNA结合蛋白hrp65为肌动蛋白结合蛋白，并表明hrp65-2同工型的C端序列能够在体外与肌动蛋白直接相互作用。体内交联和免疫共沉淀实验表明，hrp65和肌动蛋白也与活细胞相关。而且，体内施用对应于hrp65-2的C-末端序列的竞争性肽破坏了肌动蛋白-hrp65-2的相互作用，并导致了特异性和显着的转录减少，如通过吹气消退和减少的溴-UTP掺入所判断的。我们的结果表明，基于肌动蛋白的机制与大多数（如果不是全部）RNA聚合酶II基因的转录有关，并暗示需要肌动蛋白-hrp65-2相互作用才能维持细胞的正常转录活性。此外，免疫电子显微镜实验和核运行分析表明，肌动蛋白-hrp65-2复合物在转录延伸中起作用。 [参考：36]

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