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G-Quadruplexes act as sequence-dependent protein chaperones.
EMBO Reports ( IF 6.5 ) Pub Date : 2020-09-18 , DOI: 10.15252/embr.201949735
Adam Begeman 1 , Ahyun Son 1 , Theodore J Litberg 1 , Tadeusz H Wroblewski 1 , Thane Gehring 1 , Veronica Huizar Cabral 1 , Jennifer Bourne 2 , Zhenyu Xuan 3 , Scott Horowitz 1
Affiliation  

Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over 500 nucleic acid sequences’ effects on protein aggregation, we show that the holdase chaperone effect of nucleic acids is sequence‐dependent. G‐Quadruplexes prevent protein aggregation via quadruplex:protein oligomerization. They also increase the folded protein level of a biosensor in E. coli. These observations contextualize recent reports of quadruplexes playing important roles in aggregation‐related diseases, such as fragile X and amyotrophic lateral sclerosis (ALS), and provide evidence that nucleic acids have the ability to modulate the folding environment of E. coli.

中文翻译:

G-四链体起序列依赖性蛋白伴侣的作用。

维持蛋白质组健康对细胞存活很重要。核酸具有比传统伴侣蛋白更有效地防止蛋白质聚集的能力。在这项研究中,我们探索了分子伴侣活性的序列特异性。通过评估500多个核酸序列对蛋白质聚集的影响,我们发现核酸的Holdase伴侣效应是依赖序列的。G-四链体通过四链体:蛋白质寡聚防止蛋白质聚集。它们还增加了大肠杆菌中生物传感器的折叠蛋白水平。这些观察结果结合了最近有关四链体在聚集相关疾病(如脆弱X和肌萎缩性侧索硬化症(ALS))中起重要作用的报道,并提供了核酸具有调节大肠杆菌折叠环境的能力的证据。
更新日期:2020-10-05
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