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定量磷酸化蛋白质组学分析揭示了 . 对碳酸氢钠响应的机制。

Quantitative Phosphoproteomic Analysis Provides Insights into the Sodium Bicarbonate Responsiveness of .

机构信息

Key Laboratory of Soybean Biology of Chinese Education Ministry, Harbin 150030, China.

Key Laboratory of Agricultural Biological Functional Genes, Northeast Agricultural University, Harbin 150030, China.

出版信息

Biomolecules. 2023 Oct 13;13(10):1520. doi: 10.3390/biom13101520.

DOI:10.3390/biom13101520
PMID:37892202
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10605096/
Abstract

Sodium bicarbonate stress caused by NaHCO is one of the most severe abiotic stresses affecting agricultural production worldwide. However, little attention has been given to the molecular mechanisms underlying plant responses to sodium bicarbonate stress. To understand phosphorylation events in signaling pathways triggered by sodium bicarbonate stress, TMT-labeling-based quantitative phosphoproteomic analyses were performed on soybean leaf and root tissues under 50 mM NaHCO treatment. In the present study, a total of 7856 phosphopeptides were identified from cultivated soybeans ( L. Merr.), representing 3468 phosphoprotein groups, in which 2427 phosphoprotein groups were newly identified. These phosphoprotein groups contained 6326 unique high-probability phosphosites (UHPs), of which 77.2% were newly identified, increasing the current soybean phosphosite database size by 43.4%. Among the phosphopeptides found in this study, we determined 67 phosphopeptides (representing 63 phosphoprotein groups) from leaf tissue and 554 phosphopeptides (representing 487 phosphoprotein groups) from root tissue that showed significant changes in phosphorylation levels under sodium bicarbonate stress (fold change >1.2 or <0.83, respectively; < 0.05). Localization prediction showed that most phosphoproteins localized in the nucleus for both leaf and root tissues. GO and KEGG enrichment analyses showed quite different enriched functional terms between leaf and root tissues, and more pathways were enriched in the root tissue than in the leaf tissue. Moreover, a total of 53 different protein kinases and 7 protein phosphatases were identified from the differentially expressed phosphoproteins (DEPs). A protein kinase/phosphatase interactor analysis showed that the interacting proteins were mainly involved in/with transporters/membrane trafficking, transcriptional level regulation, protein level regulation, signaling/stress response, and miscellaneous functions. The results presented in this study reveal insights into the function of post-translational modification in plant responses to sodium bicarbonate stress.

摘要

碳酸氢钠胁迫(由 NaHCO 引起)是影响全球农业生产的最严重非生物胁迫之一。然而,人们对植物应对碳酸氢钠胁迫的分子机制关注甚少。为了了解碳酸氢钠胁迫引发的信号通路中的磷酸化事件,对 50 mM NaHCO 处理下的大豆叶片和根组织进行了 TMT 标记定量磷酸蛋白质组学分析。在本研究中,从栽培大豆( L. Merr.)中鉴定出了总共 7856 个磷酸肽,代表 3468 个磷酸蛋白组,其中 2427 个磷酸蛋白组是新鉴定的。这些磷酸蛋白组包含 6326 个独特的高可信度磷酸化位点(UHPs),其中 77.2%是新鉴定的,使当前大豆磷酸化位点数据库的大小增加了 43.4%。在本研究中发现的磷酸肽中,我们从叶片组织中确定了 67 个磷酸肽(代表 63 个磷酸蛋白组),从根组织中确定了 554 个磷酸肽(代表 487 个磷酸蛋白组),它们在碳酸氢钠胁迫下的磷酸化水平发生了显著变化(分别为倍数变化>1.2 或<0.83,<0.05)。定位预测显示,大多数磷酸蛋白在叶片和根组织中都定位于细胞核。GO 和 KEGG 富集分析表明,叶片组织和根组织之间存在相当不同的富集功能术语,并且在根组织中富集的途径比在叶片组织中多。此外,从差异表达磷酸蛋白(DEPs)中鉴定出了总共 53 种不同的蛋白激酶和 7 种蛋白磷酸酶。蛋白激酶/磷酸酶相互作用分析表明,相互作用蛋白主要参与/与转运体/膜运输、转录水平调节、蛋白质水平调节、信号/应激反应和杂项功能有关。本研究的结果揭示了植物应对碳酸氢钠胁迫的翻译后修饰功能的深入了解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/da2763671182/biomolecules-13-01520-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/a058ab379be0/biomolecules-13-01520-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/6aa409d59596/biomolecules-13-01520-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/52c8c5542ec4/biomolecules-13-01520-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/6ad138b392fb/biomolecules-13-01520-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/c801c5c9b818/biomolecules-13-01520-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/f4da65aea2de/biomolecules-13-01520-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/da2763671182/biomolecules-13-01520-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/a058ab379be0/biomolecules-13-01520-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/6aa409d59596/biomolecules-13-01520-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/52c8c5542ec4/biomolecules-13-01520-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/6ad138b392fb/biomolecules-13-01520-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/c801c5c9b818/biomolecules-13-01520-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/f4da65aea2de/biomolecules-13-01520-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f12/10605096/da2763671182/biomolecules-13-01520-g007.jpg

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