Jürgen Eirich, Jean-Baptiste Boyer, Laura Armbruster, Aiste Ivanauskaite, Carolina De La Torre, Thierry Meinnel, Markus Wirtz, Paula Mulo, Iris Finkemeier, Carmela Giglione
{"title":"光照变化会促进质体蛋白乙酰化标记的不同反应。","authors":"Jürgen Eirich, Jean-Baptiste Boyer, Laura Armbruster, Aiste Ivanauskaite, Carolina De La Torre, Thierry Meinnel, Markus Wirtz, Paula Mulo, Iris Finkemeier, Carmela Giglione","doi":"10.1016/j.mcpro.2024.100845","DOIUrl":null,"url":null,"abstract":"<p><p>Protein acetylation is a key co- and post-translational modification. However, how different types of acetylation respond to environmental stress is still unknown. To address this, we investigated the role of a member of the newly discovered family of plastid acetyltransferases (GNAT2), which features both lysine- and N-terminal acetyltransferase activities. Our study aimed to provide a holistic multi-omics acetylation-dependent view of plant acclimation to short-term light changes. We found that both the yield and coverage of the N-terminal acetylome remained unchanged in WT and gnat2-KO backgrounds after 2 h of exposure to high light or darkness. Similarly, no differences in transcriptome or adenylate energy charge were observed between the genotypes under the tested light conditions. In contrast, the lysine acetylome proved to be sensitive to the changes in light conditions, especially in the gnat2 background. This suggests unique strategies of plant acclimation for quick responses to environmental changes involving lysine, but not N-terminal, GNAT2-mediated acetylation activity.</p>","PeriodicalId":18712,"journal":{"name":"Molecular & Cellular Proteomics","volume":" ","pages":"100845"},"PeriodicalIF":6.1000,"publicationDate":"2024-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11546460/pdf/","citationCount":"0","resultStr":"{\"title\":\"Light Changes Promote Distinct Responses of Plastid Protein Acetylation Marks.\",\"authors\":\"Jürgen Eirich, Jean-Baptiste Boyer, Laura Armbruster, Aiste Ivanauskaite, Carolina De La Torre, Thierry Meinnel, Markus Wirtz, Paula Mulo, Iris Finkemeier, Carmela Giglione\",\"doi\":\"10.1016/j.mcpro.2024.100845\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Protein acetylation is a key co- and post-translational modification. However, how different types of acetylation respond to environmental stress is still unknown. To address this, we investigated the role of a member of the newly discovered family of plastid acetyltransferases (GNAT2), which features both lysine- and N-terminal acetyltransferase activities. Our study aimed to provide a holistic multi-omics acetylation-dependent view of plant acclimation to short-term light changes. We found that both the yield and coverage of the N-terminal acetylome remained unchanged in WT and gnat2-KO backgrounds after 2 h of exposure to high light or darkness. Similarly, no differences in transcriptome or adenylate energy charge were observed between the genotypes under the tested light conditions. In contrast, the lysine acetylome proved to be sensitive to the changes in light conditions, especially in the gnat2 background. This suggests unique strategies of plant acclimation for quick responses to environmental changes involving lysine, but not N-terminal, GNAT2-mediated acetylation activity.</p>\",\"PeriodicalId\":18712,\"journal\":{\"name\":\"Molecular & Cellular Proteomics\",\"volume\":\" \",\"pages\":\"100845\"},\"PeriodicalIF\":6.1000,\"publicationDate\":\"2024-09-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11546460/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular & Cellular Proteomics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/j.mcpro.2024.100845\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular & Cellular Proteomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/j.mcpro.2024.100845","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
引用次数: 0
摘要
蛋白质乙酰化是一种关键的共翻译和翻译后修饰。然而,不同类型的乙酰化如何应对环境胁迫仍是未知数。为了解决这个问题,我们研究了新发现的质体乙酰转移酶家族成员(GNAT2)的作用,它同时具有赖氨酸和 N 端乙酰转移酶活性。我们的研究旨在为植物适应短期光照变化提供一个多组学乙酰化依赖的整体视角。我们发现,在野生型和gnat2-敲除型背景中,暴露于强光或黑暗中两小时后,N-末端乙酰化组的产量和覆盖率均保持不变。同样,在测试的光照条件下,也没有观察到基因型之间转录组或腺苷酸能量电荷的差异。相比之下,赖氨酸乙酰组对光照条件的变化非常敏感,尤其是在gnat2背景下。这表明植物对环境变化做出快速反应的独特适应策略涉及赖氨酸,而不是 N 端 GNAT2 介导的乙酰化活性。
Light Changes Promote Distinct Responses of Plastid Protein Acetylation Marks.
Protein acetylation is a key co- and post-translational modification. However, how different types of acetylation respond to environmental stress is still unknown. To address this, we investigated the role of a member of the newly discovered family of plastid acetyltransferases (GNAT2), which features both lysine- and N-terminal acetyltransferase activities. Our study aimed to provide a holistic multi-omics acetylation-dependent view of plant acclimation to short-term light changes. We found that both the yield and coverage of the N-terminal acetylome remained unchanged in WT and gnat2-KO backgrounds after 2 h of exposure to high light or darkness. Similarly, no differences in transcriptome or adenylate energy charge were observed between the genotypes under the tested light conditions. In contrast, the lysine acetylome proved to be sensitive to the changes in light conditions, especially in the gnat2 background. This suggests unique strategies of plant acclimation for quick responses to environmental changes involving lysine, but not N-terminal, GNAT2-mediated acetylation activity.
期刊介绍:
The mission of MCP is to foster the development and applications of proteomics in both basic and translational research. MCP will publish manuscripts that report significant new biological or clinical discoveries underpinned by proteomic observations across all kingdoms of life. Manuscripts must define the biological roles played by the proteins investigated or their mechanisms of action.
The journal also emphasizes articles that describe innovative new computational methods and technological advancements that will enable future discoveries. Manuscripts describing such approaches do not have to include a solution to a biological problem, but must demonstrate that the technology works as described, is reproducible and is appropriate to uncover yet unknown protein/proteome function or properties using relevant model systems or publicly available data.
Scope:
-Fundamental studies in biology, including integrative "omics" studies, that provide mechanistic insights
-Novel experimental and computational technologies
-Proteogenomic data integration and analysis that enable greater understanding of physiology and disease processes
-Pathway and network analyses of signaling that focus on the roles of post-translational modifications
-Studies of proteome dynamics and quality controls, and their roles in disease
-Studies of evolutionary processes effecting proteome dynamics, quality and regulation
-Chemical proteomics, including mechanisms of drug action
-Proteomics of the immune system and antigen presentation/recognition
-Microbiome proteomics, host-microbe and host-pathogen interactions, and their roles in health and disease
-Clinical and translational studies of human diseases
-Metabolomics to understand functional connections between genes, proteins and phenotypes