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首页> 外文期刊>Molecular and Cellular Biology >The Carboxyl Terminus of RNA Helicase A Contains a Bidirectional Nuclear Transport Domain
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The Carboxyl Terminus of RNA Helicase A Contains a Bidirectional Nuclear Transport Domain

机译：RNA解旋酶A的羧基末端包含双向核转运域。

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Human RNA helicase A was recently identified to be a shuttle protein which interacts with the constitutive transport element (CTE) of type D retroviruses. Here we show that a domain of 110 amino acids at the carboxyl terminus of helicase A is both necessary and sufficient for nuclear localization as well as rapid nuclear export of glutathioneS-transferase fusion proteins. The import and export activities of this domain overlap but are separable by point mutations. This bidirectional nuclear transport domain (NTD) has no obvious sequence homology to previously identified nuclear import or export signals. However, the Ran-dependent nuclear import of NTD was efficiently competed by excess amounts of the nuclear localization signal (NLS) peptide from simian virus 40 large T antigen, suggesting that import is mediated by the classical NLS pathway. The nuclear export pathway accessed by NTD is insensitive to leptomycin B and thus is distinct from the leucine-rich nuclear export signal pathway mediated by CRM1.
机译：最近，人类RNA解旋酶A被确定为一种穿梭蛋白，可与D型逆转录病毒的组成型转运元件（CTE）相互作用。在这里，我们显示解旋酶A的羧基末端有110个氨基酸的结构域对于谷胱甘肽 S -转移酶融合蛋白的核定位以及快速核输出都是必要和充分的。此域的导入和导出活动重叠，但是可以通过点突变来分离。该双向核转运域（NTD）与先前确定的核输入或输出信号没有明显的序列同源性。但是，依赖于Ran的NTD核输入与来自猿猴病毒40大T抗原的过量核定位信号（NLS）肽有效竞争，这表明该输入是由经典NLS途径介导的。 NTD访问的核输出途径对瘦霉素B不敏感，因此与CRM1介导的富含亮氨酸的核输出信号途径不同。

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