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DEAD-Box蛋白eIF4A调节RNA凝集
2020-01-10 16:04

美国科罗拉多大学博尔德分校Roy Parker团队的一项最新研究发现,DEAD-Box蛋白eIF4A调节RNA凝集。相关论文2020年1月9日在线发表在《细胞》上。

应力颗粒部分地通过分子间RNA-RNA相互作用形成,并且为了更好地理解RNA凝集是如何发生的,研究人员证明了RNA在体外有效地募集到RNA或RNP凝集物的表面。研究人员证明,通过ATP依赖的RNA结合,DEAD-box蛋白eIF4A可以在体外降低RNA凝集并限制细胞中应激颗粒的形成。这定义了eIF4A限制细胞内分子间RNA-RNA相互作用的功能。这些结果为eIF4A和潜在的其他DEAD-box蛋白确立了重要的作用,因为它们是ATP依赖性RNA伴侣,可限制RNA的凝集,这类似于HSP70等蛋白质在对抗蛋白质聚集体中的功能。

据了解,应激颗粒是参与应激反应和神经退行性疾病的非翻译mRNA和蛋白质的凝集物。

附:英文原文

Title: Modulation of RNA Condensation by the DEAD-Box Protein eIF4A

Author: Devin Tauber, Gabriel Tauber, Anthony Khong, Briana Van Treeck, Jerry Pelletier, Roy Parker

Issue&Volume: January 9, 2020

Abstract: Stress granules are condensates of non-translating mRNAs and proteins involved inthe stress response and neurodegenerative diseases. Stress granules form in part throughintermolecular RNA-RNA interactions, and to better understand how RNA-based condensationoccurs, we demonstrate that RNA is effectively recruited to the surfaces of RNA orRNP condensates in vitro. We demonstrate that, through ATP-dependent RNA binding, the DEAD-box protein eIF4Areduces RNA condensation in vitro and limits stress granule formation in cells. This defines a function for eIF4A tolimit intermolecular RNA-RNA interactions in cells. These results establish an importantrole for eIF4A, and potentially other DEAD-box proteins, as ATP-dependent RNA chaperonesthat limit the condensation of RNA, analogous to the function of proteins like HSP70in combatting protein aggregates.

DOI: 10.1016/j.cell.2019.12.031

Source: https://www.cell.com/cell/fulltext/S0092-8674(19)31393-5

Cell:《细胞》,创刊于1974年。隶属于细胞出版社,最新IF:66.85
官方网址:https://www.cell.com/
投稿链接:https://www.editorialmanager.com/cell/default.aspx

本期文章:《细胞》:Online/在线发表

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