Light changes promote distinct responses of plastid protein acetylation marks
: Eirich, Jürgen; Boyer, Jean-Baptiste; Armbruster, Laura; Ivanauskaite, Aiste; De La Torre, Carolina; Meinnel, Thierry; Wirtz, Markus; Mulo, Paula; Finkemeier, Iris; Giglione, Carmela
Publisher: Elsevier BV
: 2024
: Molecular and Cellular Proteomics
: Molecular & Cellular Proteomics
: Mol Cell Proteomics
: 100845
: 23
: 11
: 1535-9476
: 1535-9484
DOI: https://doi.org/10.1016/j.mcpro.2024.100845
: https://doi.org/10.1016/j.mcpro.2024.100845
: https://research.utu.fi/converis/portal/detail/Publication/458657786
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 wild-type and gnat2-knockout backgrounds after two hours 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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This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) – Projektnummern FI 1655/4, 445970965, 469950637, 507704013 to IF and Projektnummern 235736350 and 496871662 to MW. CG acknowledges ProteoCure COST (European Cooperation in Science and Technology) action CA20113 for support. PM and AI acknowledge Academy of Finland (grant numbers 321616, 330083) and the Doctoral Programme in Molecular Life Sciences (University of Turku, Finland).
