酿酒酵母新生多肽相关复合体(NAC)亚基之间的功能异同。

IF 3.3 3区 生物学 Q3 CELL BIOLOGY
Brenda A. Schilke , Thomas Ziegelhoffer , Przemyslaw Domanski , Jaroslaw Marszalek , Bartlomiej Tomiczek , Elizabeth A. Craig
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引用次数: 0

摘要

蛋白因子在隧道出口附近与核糖体结合,促进蛋白质的运输和折叠。在真核生物中,异源二聚体新生多肽相关复合物(NAC)的含量最高,与核糖体等摩尔。酿酒酵母除了有丰富的 Nacβ1 外,还有一个次要的 β 型亚基(Nacβ2),因此有两个 NAC 异二聚体,即 α/β1 和 α/β12。额外的 beta NAC 基因是在 S. cerevisiae 系发生全基因组复制时产生的。Nacβ2 与调控 CCR4-Not 复合物的 Caf130 亚基相互作用,在翻译过程中调节编码核糖体蛋白 Rpl4 的 mRNA 的命运。我们发现,Nacβ2 在球状结构域 C 端的残基是其与 Caf130 相互作用的必要条件,也是其对缺乏 Acl4(Rpl4 的特化伴侣)的细胞生长产生负面影响的必要条件。将这些 Nacβ2 残基置换到 Nacβ1 的同源位置,可产生一种嵌合蛋白,它能与 Caf130 相互作用,并减缓缺乏 Nacβ2 的 ∆acl4 细胞的生长。此外,改变 Nacβ2 或嵌合 Nacβ1 N 末端的残基也可克服 ∆acl4 的生长缺陷。我们的研究结果符合这样一个模型,即 Nacβ2 与核糖体的结合本身或其精确定位对于 CCR4-Not 通过其与 Caf130 亚基的相互作用进行有效招募以驱动 Rpl4 mRNA 降解是必要的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Functional similarities and differences among subunits of the nascent polypeptide-associated complex (NAC) of Saccharomyces cerevisiae
Protein factors bind ribosomes near the tunnel exit, facilitating protein trafficking and folding. In eukaryotes, the heterodimeric nascent polypeptide-associated complex (NAC) is the most abundant—equimolar to ribosomes. Saccharomyces cerevisiae has a minor β-type subunit (Nacβ2) in addition to abundant Nacβ1, and therefore two NAC heterodimers, α/β1 and α/β12. The additional beta NAC gene arose at the time of the whole genome duplication that occurred in the S. cerevisiae lineage. Nacβ2 has been implicated in regulating the fate of messenger RNA encoding ribosomal protein Rpl4 during translation via its interaction with the Caf130 subunit of the regulatory CCR4-Not complex. We found that Nacβ2 residues just C-terminal to the globular domain are required for its interaction with Caf130 and its negative effect on the growth of cells lacking Acl4, the specialized chaperone for Rpl4. Substitution of these Nacβ2 residues at homologous positions in Nacβ1 results in a chimeric protein that interacts with Caf130 and slows the growth of ∆acl4 cells lacking Nacβ2. Furthermore, alteration of residues in the N-terminus of Nacβ2 or chimeric Nacβ1 previously shown to affect ribosome binding overcomes the growth defect of ∆acl4. Our results are consistent with a model in which Nacβ2’s ribosome association per se or its precise positioning is necessary for productive recruitment of CCR4-Not via its interaction with the Caf130 subunit to drive Rpl4 messenger RNA degradation.
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来源期刊
Cell Stress & Chaperones
Cell Stress & Chaperones 生物-细胞生物学
CiteScore
7.60
自引率
2.60%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Cell Stress and Chaperones is an integrative journal that bridges the gap between laboratory model systems and natural populations. The journal captures the eclectic spirit of the cellular stress response field in a single, concentrated source of current information. Major emphasis is placed on the effects of climate change on individual species in the natural environment and their capacity to adapt. This emphasis expands our focus on stress biology and medicine by linking climate change effects to research on cellular stress responses of animals, micro-organisms and plants.
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