Communication between RACK1/Asc1 and uS3 (Rps3) is essential for RACK1/Asc1 function in yeast Saccharomyces cerevisiae.
Communication between RACK1/Asc1 and uS3 (Rps3) is essential for RACK1/Asc1 function in yeast Saccharomyces cerevisiae.
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DOI：
10.1016/j.gene.2019.04.087
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发表时间：
2019-07
期刊：
影响因子：
3.5
通讯作者：
Nishant Singh;Supriya Jindal;Arnab Ghosh;A. Komar
中科院分区：
文献类型：
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作者：
Nishant Singh;Supriya Jindal;Arnab Ghosh;A. Komar
活化c激酶受体（RACK 1，Asc 1）是一种真核生物核糖体蛋白，位于mRNA出口通道附近的40 S亚基的头部区域。这种WD重复β推进器蛋白作为信号分子，参与代谢调节、细胞周期进程和翻译控制。然而，RACK 1募集和与40 S核糖体亚基稳定关联的确切细节仍然只有部分已知。酵母（Saccharomyces cerevisiae）核糖体的X射线分析揭示RACK 1螺旋桨叶片（4-5）与核糖体蛋白S3（uS 3家族）的真核生物特异性C-末端结构域（CTD）相互作用。为了检查这种相互作用的功能意义，我们产生了含有uS 3的C末端缺失的突变酵母菌株。我们发现从uS 3-CTD中删除20个C-末端残基（与叶片4-5相互作用）消除了RACK 1与核糖体的结合。具有截短的uS 3-CTD的菌株表现出与RACK 1 Δ菌株相似的细胞生长和蛋白质合成受损，从而表明uS 3-CTD不仅对于RACK 1与核糖体的募集和缔合至关重要，而且对于其细胞内功能也至关重要。我们认为，真核生物特异性RACK 1-uS 3相互作用已演变为核糖体和细胞信号通路之间的联系。
The receptor for activated c-kinase (RACK1, Asc1 in yeast) is a eukaryotic ribosomal protein located in the head region of the 40S subunit near the mRNA exit channel. This WD-repeat β-propeller protein acts as a signaling molecule and is involved in metabolic regulation, cell cycle progression, and translational control. However, the exact details of the RACK1 recruitment and stable association with the 40S ribosomal subunit remain only partially known. X-ray analyses of the yeast,Saccharomyces cerevisiae, ribosome revealed that the RACK1 propeller blade (4–5) interacts with the eukaryote-specific C-terminal domain (CTD) of ribosomal protein S3 (uS3 family). To check the functional significance of this interaction, we generated mutant yeast strains harboring C-terminal deletions of uS3. We found that deletion of the 20 C-terminal residues (interacting with blade 4–5) from the uS3-CTD abrogates RACK1 binding to the ribosome. Strains with truncated uS3-CTD exhibited compromised cellular growth and protein synthesis similar to that ofRACK1Δstrain, thus suggesting that the uS3-CTD is crucial not only for the recruitment and association of RACK1 with the ribosome, but also for its intracellular function. We suggest that eukaryote-specific RACK1-uS3 interaction has evolved to act as a link between the ribosome and the cellular signaling pathways.