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Crosstalk of Phosphorylation and Arginine Methylation in Disordered SRGG Repeats of Saccharomycescerevisiae Fibrillarin and Its Association with Nucleolar Localization.
Journal of Molecular Biology ( IF 4.7 ) Pub Date : 2019-11-20 , DOI: 10.1016/j.jmb.2019.11.006 Daniela-Lee Smith 1 , Melissa A Erce 1 , Yu-Wen Lai 1 , Florence Tomasetig 2 , Gene Hart-Smith 1 , Joshua J Hamey 1 , Marc R Wilkins 1
Journal of Molecular Biology ( IF 4.7 ) Pub Date : 2019-11-20 , DOI: 10.1016/j.jmb.2019.11.006 Daniela-Lee Smith 1 , Melissa A Erce 1 , Yu-Wen Lai 1 , Florence Tomasetig 2 , Gene Hart-Smith 1 , Joshua J Hamey 1 , Marc R Wilkins 1
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Crosstalk exists when two or more post-translational modifications, nearby in sequence or 3D space, affect each other or a protein's interactions. Saccharomyces cerevisiae protein Npl3p has six repeats of sequence SRGG, in a disordered domain, which can carry arginine methylation and serine phosphorylation. Crosstalk of the modifications controls Npl3p interactions with nuclear import, export, and other proteins. Here, we asked whether repeated SRGG motifs existed in other S. cerevisiae proteins and whether they serve a related function. Two other proteins had multiple SRGG motifs: Nop1p (fibrillarin) and Gar1p, both nucleolar proteins, which had nine and four motifs, respectively. For Nop1p, we first showed it to be extensively methylated in vivo. We then showed that the Nop1p SRGG motif is subjected to methylation by Hmt1p, phosphorylation by Sky1p, and Glc7p dephosphorylation and that there is crosstalk whereby phosphorylation blocks methylation. This is consistent with our recent motif analysis of Hmt1p, which revealed a negative specificity for acidic residues at -1 and -2 positions. On knockout of HMT1, Nop1p-GFP localization was not typically nucleolar. Conditional two-hybrid analysis, of Nop1p with C/D box small ribonuclear proteins Nop56p and Nop58p, suggested this may be associated with decreased protein-protein interactions on loss of arginine methylation. The effect of SRGG phosphorylation on the interactions of Nop1p remains unknown yet was predicted to cause a structural disorder-to-order transition in the Nop1p N-terminal domain. The SRGG motif is one of very few examples of modification crosstalk that has related functions in multiple proteins from the same species.
中文翻译：
酿酒酵母原纤维蛋白的无序SRGG重复序列中磷酸化和精氨酸甲基化的串扰及其与核仁定位的关系。
当序列或3D空间附近的两个或多个翻译后修饰相互影响或影响蛋白质相互作用时，就会存在串扰。酿酒酵母蛋白Npl3p在无序域中具有SRGG序列的六个重复序列，可以携带精氨酸甲基化和丝氨酸磷酸化。修饰的串扰控制Npl3p与核输入，输出和其他蛋白质的相互作用。在这里，我们询问在其他酿酒酵母蛋白中是否存在重复的SRGG基序，以及它们是否具有相关功能。另外两个蛋白具有多个SRGG基序：Nop1p（原纤维蛋白）和Gar1p，均为核仁蛋白，分别具有9个和4个基序。对于Nop1p，我们首先证明了它在体内被广泛甲基化。然后，我们表明Nop1p SRGG基序受Hmt1p甲基化，通过Sky1p进行磷酸化，以及Glc7p进行去磷酸化，并且存在串扰，因此磷酸化会阻止甲基化。这与我们最近对Hmt1p进行的基序分析相一致，后者对-1和-2位置的酸性残基显示出负特异性。敲除HMT1时，Nop1p-GFP的定位通常不是核仁。对具有C / D盒小核糖蛋白Nop56p和Nop58p的Nop1p进行条件性两杂交分析，表明这可能与精氨酸甲基化丧失时蛋白质-蛋白质相互作用降低有关。SRGG磷酸化对Nop1p相互作用的影响仍然未知，但据预测会在Nop1p N端结构域引起结构无序到有序过渡。
更新日期：2019-11-20
中文翻译：
酿酒酵母原纤维蛋白的无序SRGG重复序列中磷酸化和精氨酸甲基化的串扰及其与核仁定位的关系。
当序列或3D空间附近的两个或多个翻译后修饰相互影响或影响蛋白质相互作用时，就会存在串扰。酿酒酵母蛋白Npl3p在无序域中具有SRGG序列的六个重复序列，可以携带精氨酸甲基化和丝氨酸磷酸化。修饰的串扰控制Npl3p与核输入，输出和其他蛋白质的相互作用。在这里，我们询问在其他酿酒酵母蛋白中是否存在重复的SRGG基序，以及它们是否具有相关功能。另外两个蛋白具有多个SRGG基序：Nop1p（原纤维蛋白）和Gar1p，均为核仁蛋白，分别具有9个和4个基序。对于Nop1p，我们首先证明了它在体内被广泛甲基化。然后，我们表明Nop1p SRGG基序受Hmt1p甲基化，通过Sky1p进行磷酸化，以及Glc7p进行去磷酸化，并且存在串扰，因此磷酸化会阻止甲基化。这与我们最近对Hmt1p进行的基序分析相一致，后者对-1和-2位置的酸性残基显示出负特异性。敲除HMT1时，Nop1p-GFP的定位通常不是核仁。对具有C / D盒小核糖蛋白Nop56p和Nop58p的Nop1p进行条件性两杂交分析，表明这可能与精氨酸甲基化丧失时蛋白质-蛋白质相互作用降低有关。SRGG磷酸化对Nop1p相互作用的影响仍然未知，但据预测会在Nop1p N端结构域引起结构无序到有序过渡。
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