Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1.
Analysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1.
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DOI：
10.1371/journal.pone.0164773
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发表时间：
2016
期刊：
影响因子：
3.7
通讯作者：
Irie K
中科院分区：
文献类型：
--
作者：
Lien PT;Izumikawa K;Muroi K;Irie K;Suda Y;Irie K
Scd 6是人RAP 55的酵母同源物，是信使核糖核蛋白（mRNP）的一个组分，其通过与翻译起始因子结合来抑制翻译，并且与结合伴侣Edc 3和Dhh 1一起沿着是去帽激活剂。在此，我们报告，Scd 6是内源性蛋白质精氨酸甲基转移酶，Hmt 1，在芽殖酵母酿酒酵母的底物。质谱分析表明，几个精氨酸残基内的Scd 6 RGG基序，这是重要的mRNA结合，甲基化的Hmt 1依赖的方式。在葡萄糖饥饿等应激条件下，Scd 6定位于细胞质加工体（P-体），其中抑制的mRNP和未翻译的mRNA积累。在hmt 1缺失突变体和存在甲基化缺陷的Scd 6取代的情况下，Scd 6定位于P体受损。此外，scd 6和dhh 1的缺失导致了严重的高温合成生长缺陷。Scd 6甲基化缺陷突变抑制了scd 6 dhh 1双突变体的表型缺陷，而甲基化模拟突变则没有抑制作用，提示精氨酸甲基化可能负调控Scd 6与dhh 1相关的功能。因此，目前的数据表明，基于Hmt 1的精氨酸甲基化是Scd 6定位和功能所必需的。
Scd6, a yeast homologue of human RAP55, is a component of messenger ribonucleoproteins (mRNPs) that repress translation by binding to translation initiation factors, and also is a decapping activator along with the binding partners Edc3 and Dhh1. Herein, we report that Scd6 is a substrate of the intrinsic protein arginine methyltransferase, Hmt1, in budding yeast Saccharomyces cerevisiae. Mass spectrometric analysis revealed that several arginine residues within the Scd6 RGG motif, which is important for mRNA binding, were methylated in Hmt1 dependent manner. Under stress conditions such as glucose starvation, Scd6 localized to cytoplasmic processing bodies (P-bodies) wherein translationally repressed mRNPs and untranslated mRNAs accumulate. Localization of Scd6 to P-bodies was impaired in hmt1 deletion mutant and in the presence of methylation-deficient substitution of Scd6. In addition, deletion of scd6 and dhh1 led to severe synthetic growth defect at high temperature. Methylation-deficient mutation of Scd6 suppressed the phenotypic defects of scd6 dhh1 double mutant, whereas methylation-mimic mutation did not, suggesting that the arginine methylation might negatively regulate Scd6 function relating to Dhh1. Therefore, the present data suggest that Hmt1-based arginine methylation is required for Scd6 localization and function.
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