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植物中的 R-甲基化:调控植物发育和响应环境的关键因子。

R-Methylation in Plants: A Key Regulator of Plant Development and Response to the Environment.

机构信息

Crop Biotechnics, Department of Biosystems, KU Leuven, 3000 Leuven, Belgium.

KU Leuven Plant Institute (LPI), KU Leuven, 3000 Leuven, Belgium.

出版信息

Int J Mol Sci. 2024 Sep 14;25(18):9937. doi: 10.3390/ijms25189937.

DOI:10.3390/ijms25189937
PMID:39337424
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11432338/
Abstract

Although arginine methylation (R-methylation) is one of the most important post-translational modifications (PTMs) conserved in eukaryotes, it has not been studied to the same extent as phosphorylation and ubiquitylation. Technical constraints, which are in the process of being resolved, may partly explain this lack of success. Our knowledge of R-methylation has recently evolved considerably, particularly in metazoans, where misregulation of the enzymes that deposit this PTM is implicated in several diseases and cancers. Indeed, the roles of R-methylation have been highlighted through the analyses of the main actors of this pathway: the PRMT writer enzymes, the TUDOR reader proteins, and potential "eraser" enzymes. In contrast, R-methylation has been much less studied in plants. Even so, it has been shown that R-methylation in plants, as in animals, regulates housekeeping processes such as transcription, RNA silencing, splicing, ribosome biogenesis, and DNA damage. R-methylation has recently been highlighted in the regulation of membrane-free organelles in animals, but this role has not yet been demonstrated in plants. The identified R-met targets modulate key biological processes such as flowering, shoot and root development, and responses to abiotic and biotic stresses. Finally, arginine demethylases activity has mostly been identified in vitro, so further studies are needed to unravel the mechanism of arginine demethylation.

摘要

尽管精氨酸甲基化(R-甲基化)是真核生物中最保守的一种翻译后修饰(PTM),但它的研究程度不如磷酸化和泛素化。正在解决的技术限制可能部分解释了这种缺乏成功的原因。我们对 R-甲基化的认识最近有了相当大的发展,特别是在后生动物中,沉积这种 PTM 的酶的失调与几种疾病和癌症有关。事实上,通过对该途径的主要参与者:PRMT 写入酶、TUDOR 读取蛋白和潜在的“橡皮擦”酶的分析,突显了 R-甲基化的作用。相比之下,R-甲基化在植物中的研究要少得多。即便如此,已经表明植物中的 R-甲基化与动物中的一样,调节转录、RNA 沉默、剪接、核糖体生物发生和 DNA 损伤等管家过程。R-甲基化最近在动物中无膜细胞器的调节中得到了强调,但这一作用尚未在植物中得到证明。已鉴定的 R-met 靶标调节关键的生物学过程,如开花、茎和根的发育以及对非生物和生物胁迫的反应。最后,精氨酸去甲基酶的活性主要在体外被鉴定,因此需要进一步的研究来阐明精氨酸去甲基化的机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e455/11432338/ef1467263791/ijms-25-09937-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e455/11432338/1c073318b9cd/ijms-25-09937-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e455/11432338/ef1467263791/ijms-25-09937-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e455/11432338/1c073318b9cd/ijms-25-09937-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e455/11432338/ef1467263791/ijms-25-09937-g003.jpg

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Arabidopsis AGO1 N-terminal extension acts as an essential hub for PRMT5 interaction and post-translational modifications.拟南芥 AGO1 N 端延伸区作为 PRMT5 相互作用和翻译后修饰的必需枢纽。
Nucleic Acids Res. 2024 Aug 12;52(14):8466-8482. doi: 10.1093/nar/gkae387.
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SISTER OF FCA physically associates with SKB1 to regulate flowering time in Arabidopsis thaliana.
FCA 的姐妹蛋白 SKB1 与 SKB1 相互作用,共同调控拟南芥的开花时间。
BMC Plant Biol. 2024 Mar 15;24(1):188. doi: 10.1186/s12870-024-04887-y.
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The unique dual targeting of AGO1 by two types of PRMT enzymes promotes phasiRNA loading in Arabidopsis thaliana.两种 PRMT 酶对 AGO1 的独特双重靶向促进了拟南芥 phasiRNA 的加载。
Nucleic Acids Res. 2024 Mar 21;52(5):2480-2497. doi: 10.1093/nar/gkae045.
5
Light controls mesophyll-specific post-transcriptional splicing of photoregulatory genes by AtPRMT5.光通过AtPRMT5控制光调节基因的叶肉特异性转录后剪接。
Proc Natl Acad Sci U S A. 2024 Feb 6;121(6):e2317408121. doi: 10.1073/pnas.2317408121. Epub 2024 Jan 29.
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JMJD6 protects against isoproterenol-induced cardiac hypertrophy via inhibition of NF-κB activation by demethylating R149 of the p65 subunit.JMJD6 通过去甲基化 p65 亚基的 R149 抑制 NF-κB 激活,从而防止异丙肾上腺素诱导的心肌肥厚。
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The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.所有人类 KDM5 JmjC 去甲基酶的催化结构域都催化 N-甲基精氨酸去甲基化。
FEBS Lett. 2023 Apr;597(7):933-946. doi: 10.1002/1873-3468.14586. Epub 2023 Feb 7.
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