乙酰化
质体
乙酰转移酶
赖氨酸
转录组
适应
乙酰转移酶
生物
生物化学
表观遗传学
化学
遗传学
基因
基因表达
氨基酸
叶绿体
作者
Jürgen Eirich,Jean-Baptiste Boyer,Laura Armbruster,Aiste Ivanauskaite,Carolina De La Torre,Thierry Meinnel,Markus Wirtz,Paula Mulo,Iris Finkemeier,Carmela Giglione
标识
DOI:10.1016/j.mcpro.2024.100845
摘要
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.
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