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The dynamics of the alternatively spliced NOL7 gene products and role in nucleolar architecture

机译：交替剪接的NOL7基因产物的动力学及其在核仁结构中的作用

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摘要

Three alternatively spliced forms of the human NOL7 gene coding for relatively small proteins were identified. The two shorter forms were generated by intron retention events, and each isoform was differently localized within the cell. The NOL7-SP1 long form (29 kD) localized to the nucleolus, SP2 was nucleoplasmic, while SP3 was distributed throughout the whole cell. NOL7-SP1 was confined to the nucleolar granular component, and during cell division disassociated from the nucleolus. Knockdown of NOL7-SP1 levels abrogated nucleolar architecture, in particular the internal regions, and reduced cell proliferation. Analysis of the nucleolar dynamics of the SP1 protein during interphase showed nucleolar high binding affinity. Dissection of protein domains showed that nucleolar targeting was mediated by a unique C-terminal nucleolar localization sequence (NoLS). However, this sequence was not sufficient for conferring high binding affinity, which required additional regions of the protein. Our analysis shows that NOL7 is important for maintaining internal nucleolar structure and cell growth rates, and that while specific protein localization can be obtained by specific short localization motifs, nucleolar residency through binding must be mediated by a synergistic combination of protein modules.
机译：鉴定了编码相对较小蛋白质的人NOL7基因的三种剪接形式。通过内含子保留事件产生了两个较短的形式，并且每个同工型在细胞内的定位不同。 NOL7-SP1长型（29 kD）定位于核仁，SP2是核质的，而SP3则分布在整个细胞中。 NOL7-SP1局限于核仁颗粒成分，并且在细胞分裂过程中与核仁分离。降低NOL7-SP1水平可废除核仁结构，尤其是内部区域，并减少细胞增殖。在相间期SP1蛋白的核仁动力学分析表明核仁高结合亲和力。蛋白质结构域的解剖表明，核仁靶向是由独特的C末端核仁定位序列（NoLS）介导的。但是，该序列不足以赋予高结合亲和力，这需要蛋白质的其他区域。我们的分析表明，NOL7对于维持内部核仁结构和细胞生长速率很重要，并且虽然可以通过特定的短定位基序获得特定的蛋白质定位，但通过结合的核仁驻留必须由蛋白质模块的协同组合来介导。

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