Betaproteobacteria Comamonas testosteroni 的冬眠促进因子不能诱导 100S 核糖体的形成,但能稳定 70S 核糖体颗粒。

IF 16.4 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Masami Ueta, Akira Wada, Chieko Wada
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引用次数: 0

摘要

细菌在养分耗尽等压力条件下会采取多种方式求生。其中一种应对方法是形成冬眠的 100S 核糖体,这是一种翻译不活跃的 70S 二聚体。在伽马蛋白细菌(肠杆菌科)中,100S 核糖体的形成需要核糖体调节因子(RMF)和短冬眠促进因子(HPF),而在大多数细菌中,它只由长 HPF 介导。在这里,我们研究了 Comamonas testosteroni 的 HPFs 的作用。C. testosteroni有两个长度不同的HPF同源基因(CtHPF-125和CtHPF-119)。CtHPF-125 在静止期被诱导,而 CtHPF-119 在许多其他贝特蛋白杆菌中保留,在本文使用的培养条件下不表达。与短 HPF 和 RMF 以及长 HPF 不同,CtHPF-125 不能形成 100S 核糖体。我们首先构建了 Cthpf-125 基因缺失突变体。当缺失突变体在静止期生长时,70S颗粒的降解速度比野生株更快。CtHPF-125有助于稳定70S核糖体。CtHPF-125和CtHPF-119都通过体外转录-翻译抑制蛋白质合成。我们的研究结果表明,CtHPF-125能与核糖体结合,稳定70S核糖体,抑制翻译而不形成100S核糖体,有助于延长生命。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The hibernation promoting factor of Betaproteobacteria Comamonas testosteroni cannot induce 100S ribosome formation but stabilizes 70S ribosomal particles

The hibernation promoting factor of Betaproteobacteria Comamonas testosteroni cannot induce 100S ribosome formation but stabilizes 70S ribosomal particles

Bacteria use several means to survive under stress conditions such as nutrient depletion. One such response is the formation of hibernating 100S ribosomes, which are translationally inactive 70S dimers. In Gammaproteobacteria (Enterobacterales), 100S ribosome formation requires ribosome modulation factor (RMF) and short hibernation promoting factor (HPF), whereas it is mediated by only long HPF in the majority of bacteria. Here, we investigated the role of HPFs of Comamonas testosteroni, which belongs to the Betaproteobacteria with common ancestor to the Gammaproteobacteria. C. testosteroni has two genes of HPF homologs of differing length (CtHPF-125 and CtHPF-119). CtHPF-125 was induced in the stationary phase, whereas CtHPF-119 conserved in many other Betaproteobacteria was not expressed in the culture conditions used here. Unlike short HPF and RMF, and long HPF, CtHPF-125 could not form 100S ribosome. We first constructed the deletion mutant of Cthpf-125 gene. When the deletion mutant grows in the stationary phase, 70S particles were degraded faster than in the wild strain. CtHPF-125 contributes to stabilizing the 70S ribosome. CtHPF-125 and CtHPF-119 both inhibited protein synthesis by transcription-translation in vitro. Our findings suggest that CtHPF-125 binds to ribosome, and stabilizes 70S ribosomes, inhibits translation without forming 100S ribosomes and supports prolonging life.

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来源期刊
Accounts of Chemical Research
Accounts of Chemical Research 化学-化学综合
CiteScore
31.40
自引率
1.10%
发文量
312
审稿时长
2 months
期刊介绍: Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.
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