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Systematic quantitative analysis of ribosome inventory during nutrient stress

机译：营养应激期间核糖体库存的系统定量分析

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摘要

Mammalian cells reorganize their proteomes in response to nutrient stress through translational suppression and degradative mechanisms using the proteasome and autophagy systems(1,2). Ribosomes are central targets of this response, asthey are responsible for translation and subject to lysosomal turnover during nutrient stress(3-5). The abundance of ribosomal (r)-proteins (around 6% of the proteome; 10(7) copies per cell)(6,7) and their high arginine and lysine content has led to the hypothesis that they are selectively used as a source of basic amino acids during nutrient stress through autophagy(4,7). However, the relative contributions of translational and degradative mechanisms to the control of r-protein abundance during acute stress responses is poorly understood, as is the extent to which r-proteins are used to generate amino acids when specific building blocks are limited(7). Here, we integrate quantitative global translatome and degradome proteomics(8) with genetically encoded Ribo-Keima(5) and Ribo-Halo reporters to interrogate r-protein homeostasis with and without active autophagy. In conditions of acute nutrient stress, cells strongly suppress the translation of r-proteins, but, notably, r-protein degradation occurs largely through non-autophagic pathways. Simultaneously, the decrease in r-protein abundance is compensated for by a reduced dilution of pre-existing ribosomes and a reduction in cell volume, thereby maintaining the density of ribosomes within single cells. Withdrawal of basic or hydrophobic amino acids induces translational repression without differential induction of ribophagy, indicating that ribophagy is not used to selectively produce basic amino acids during acute nutrient stress. We present a quantitative framework that describes the contributions of biosynthetic and degradative mechanisms to r-protein abundance and proteome remodelling in conditions of nutrient stress.
机译：哺乳动物细胞响应于使用蛋白酶体和自噬系统（1,2）的转化抑制和降解机制响应营养胁迫而重新组织蛋白质蛋白酶。核糖体是这种反应的中央靶标，Asthey负责翻译，并在营养应激（3-5）期间受溶酶体的转换。核糖体（R） - 蛋白质的丰富（蛋白质组的约6％; 10（7）个拷贝每种细胞）（6,7）和它们的高精度和赖氨酸含量导致了它们被选择性地用作源的假设通过自噬营养胁迫期间的碱性氨基酸（4,7）。然而，平移和降解机制对急性应激响应期间对R蛋白丰度控制的相对贡献较差，而r-蛋白用于产生氨基酸的程度，当特定的构建块有限时（7） 。在此，我们将定量全局翻译和降低蛋白质组学（8）与遗传编码的核武器 - keima（5）和核武器 - 晕记者一起询问r-inder-poceostasis，无活性自噬。在急性营养应激的条件下，细胞强制抑制R蛋白的翻译，但值得注意的是，r蛋白降解主要通过非自噬途径发生。同时，通过减少预先存在的核糖体和细胞体积的降低来补偿R蛋白丰度的降低，从而保持单细胞内的核糖体密度。取出碱性或疏水性氨基酸诱导转化抑制，无差异诱导核化性，表明核经核不用于在急性营养应激期间选择性地产生碱性氨基酸。我们提出了一种定量框架，其描述了生物合成和降解机制在营养应激条件下对R蛋白丰度和蛋白质组重塑的贡献。

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  • 来源
    《Nature》 |2020年第7815期|303-309|共7页
  • 作者

    An Heeseon; Ordureau Alban; Koerner Maria; Paulo Joao A.; Harper J. Wade;

  • 作者单位

    Harvard Med Sch Blavatnik Inst Dept Cell Biol Boston MA 02115 USA;

    Harvard Med Sch Blavatnik Inst Dept Cell Biol Boston MA 02115 USA;

    Harvard Med Sch Blavatnik Inst Dept Cell Biol Boston MA 02115 USA|Univ Wurzburg Dept Biochem Wurzburg Germany;

    Harvard Med Sch Blavatnik Inst Dept Cell Biol Boston MA 02115 USA;

    Harvard Med Sch Blavatnik Inst Dept Cell Biol Boston MA 02115 USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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