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核糖核蛋白颗粒:在应激与转座元件之间。

Ribonucleoprotein Granules: Between Stress and Transposable Elements.

机构信息

Department of Biological Sciences, Kangwon National University, Chuncheon 24341, Republic of Korea.

Department of Biochemistry, Kangwon National University, Chuncheon 24341, Republic of Korea.

出版信息

Biomolecules. 2023 Jun 23;13(7):1027. doi: 10.3390/biom13071027.

DOI:10.3390/biom13071027
PMID:37509063
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10377603/
Abstract

Transposable elements (TEs) are DNA sequences that can transpose and replicate within the genome, leading to genetic changes that affect various aspects of host biology. Evolutionarily, hosts have also developed molecular mechanisms to suppress TEs at the transcriptional and post-transcriptional levels. Recent studies suggest that stress-induced formation of ribonucleoprotein (RNP) granules, including stress granule (SG) and processing body (P-body), can play a role in the sequestration of TEs to prevent transposition, suggesting an additional layer of the regulatory mechanism for TEs. RNP granules have been shown to contain factors involved in RNA regulation, including mRNA decay enzymes, RNA-binding proteins, and noncoding RNAs, which could potentially contribute to the regulation of TEs. Therefore, understanding the interplay between TEs and RNP granules is crucial for elucidating the mechanisms for maintaining genomic stability and controlling gene expression. In this review, we provide a brief overview of the current knowledge regarding the interplay between TEs and RNP granules, proposing RNP granules as a novel layer of the regulatory mechanism for TEs during stress.

摘要

转座元件 (TEs) 是能够在基因组内转座和复制的 DNA 序列,导致影响宿主生物学各个方面的遗传变化。从进化的角度来看,宿主还开发了分子机制来在转录和转录后水平抑制 TEs。最近的研究表明,应激诱导的核糖核蛋白 (RNP) 颗粒的形成,包括应激颗粒 (SG) 和处理体 (P 体),可以在隔离 TEs 以防止转座方面发挥作用,这表明 TEs 的调控机制增加了一个额外的层面。已经表明 RNP 颗粒包含参与 RNA 调节的因子,包括 mRNA 降解酶、RNA 结合蛋白和非编码 RNA,这可能有助于 TEs 的调节。因此,了解 TEs 和 RNP 颗粒之间的相互作用对于阐明维持基因组稳定性和控制基因表达的机制至关重要。在这篇综述中,我们简要概述了 TEs 和 RNP 颗粒之间相互作用的最新知识,提出 RNP 颗粒作为应激期间 TEs 调控机制的一个新层面。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/091c/10377603/8e32e277ce7a/biomolecules-13-01027-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/091c/10377603/9027159a347f/biomolecules-13-01027-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/091c/10377603/8e32e277ce7a/biomolecules-13-01027-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/091c/10377603/9027159a347f/biomolecules-13-01027-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/091c/10377603/8e32e277ce7a/biomolecules-13-01027-g002.jpg

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SARS-CoV-2 N Protein Antagonizes Stress Granule Assembly and IFN Production by Interacting with G3BPs to Facilitate Viral Replication.
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