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Principles of protein targeting to the nucleolus

机译：靶向核仁的蛋白质原理

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The nucleolus is the hallmark of nuclear compartmentalization and has been shown to exert multiple roles in cellular metabolism besides its main function as the place of rRNA synthesis and assembly of ribosomes. Nucleolar proteins dynamically localize and accumulate in this nuclear compartment relative to the surrounding nucleoplasm. In this study, we have assessed the molecular requirements that are necessary and sufficient for the localization and accumulation of peptides and proteins inside the nucleoli of living cells. The data showed that positively charged peptide entities composed of arginines alone and with an isoelectric point at and above 12.6 are necessary and sufficient for mediating significant nucleolar accumulation. A threshold of 6 arginines is necessary for peptides to accumulate in nucleoli, but already 4 arginines are sufficient when fused within 15 amino acid residues of a nuclear localization signal of a protein. Using a pH sensitive dye, we found that the nucleolar compartment is particularly acidic when compared to the surrounding nucleoplasm and, hence, provides the ideal electrochemical environment to bind poly-arginine containing proteins. In fact, we found that oligo-arginine peptides and GFP fusions bind RNA in vitro. Consistent with RNA being the main binding partner for arginines in the nucleolus, we found that the same principles apply to cells from insects to man, indicating that this mechanism is highly conserved throughout evolution.
机译：核仁是核区室化的标志，已被证明在细胞代谢中起着多种作用，除了其主要功能是rRNA合成和核糖体的组装。核仁蛋白相对于周围核质动态地定位并积累在该核区室中。在这项研究中，我们评估了活细胞核仁中肽和蛋白质的定位和积累所需的分子需求。数据表明，仅由精氨酸组成且带等电点为12.6或更高的带正电荷的肽实体对于介导明显的核仁积累是必要和充分的。肽要在核仁中积累，必须有6个精氨酸阈值，但是当融合在蛋白质核定位信号的15个氨基酸残基中时，已经有4个精氨酸就足够了。使用pH敏感染料，我们发现与周围的核质相比，核仁区特别酸性，因此，它为结合含聚精氨酸的蛋白质提供了理想的电化学环境。实际上，我们发现寡精氨酸肽和GFP融合体在体外结合RNA。与RNA是核仁中精氨酸的主要结合伴侣相一致，我们发现相同的原理适用于从昆虫到人的细胞，这表明这种机制在整个进化过程中都是高度保守的。

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