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A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes

机译:伴侣SSB-RAC和NAC新生多肽相关复合物在核糖体上的双重功能

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The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide–associated complex (NAC), another ribosome-tethered system, is functionally connected to SSB–RAC and the cytosolic Hsp70 network. Simultaneous deletions of genes encoding NAC and SSB caused conditional loss of cell viability under protein-folding stress conditions. Furthermore, NAC mutations revealed genetic interaction with a deletion of Sse1, a nucleotide exchange factor regulating the cytosolic Hsp70 network. Cells lacking SSB or Sse1 showed protein aggregation, which is enhanced by additional loss of NAC; however, these mutants differ in their potential client repertoire. Aggregation of ribosomal proteins and biogenesis factors accompanied by a pronounced deficiency in ribosomal particles and translating ribosomes only occurs in ssbΔ and nacΔssbΔ cells, suggesting that SSB and NAC control ribosome biogenesis. Thus, SSB–RAC and NAC assist protein folding and likewise have important functions for regulation of ribosome levels. These findings emphasize the concept that ribosome production is coordinated with the protein-folding capacity of ribosome-associated chaperones.
机译:酵母Hsp70 / 40系统SSB-RAC(应力70 B-核糖体相关复合物)与核糖体结合,并接触新生的多肽以协助共翻译折叠。在这项研究中,我们证明了新生的多肽相关复合物(NAC),另一个核糖体束缚系统,功能上与SSB-RAC和胞质Hsp70网络连接。编码NAC和SSB的基因的同时缺失导致蛋白质折叠胁迫条件下细胞活力的条件性丧失。此外,NAC突变揭示了与Sse1缺失的遗传相互作用,Sse1是调节细胞质Hsp70网络的核苷酸交换因子。缺少SSB或Sse1的细胞显示出蛋白质聚集,而NAC的额外丢失则增强了蛋白质聚集。但是,这些突变体的潜在客户构成不同。核糖体蛋白和生物发生因子的聚集,伴随着核糖体颗粒和翻译核糖体的明显缺乏,仅在ssbΔ和nacΔssbb细胞中发生,表明SSB和NAC控制着核糖体的生物发生。因此,SSB–RAC和NAC有助于蛋白质折叠,并且同样具有调节核糖体水平的重要功能。这些发现强调了核糖体生产与核糖体相关伴侣蛋白的蛋白质折叠能力相协调的概念。

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