Dataset Information

Arabidopsis thaliana N-terminal Acetylome

ABSTRACT: Quantitative study of the N-terminal acetylome variations in Arabidopsis thaliana, looking at the effect of a N-acetyltransferase KO.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Rosette

SUBMITTER: Jean Baptiste BOYER

LAB HEAD: Carmela GIGLIONE

PROVIDER: PXD016496 | Pride | 2020-07-13

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20190423_SCX_ERACAPS_PM_d3Ac_WT_RepBio4_Frac_02.raw	Raw
	20190423_SCX_ERACAPS_PM_d3Ac_WT_RepBio4_Frac_03.raw	Raw
	20190423_SCX_ERACAPS_PM_d3Ac_WT_RepBio4_Frac_04.raw	Raw
	20190423_SCX_ERACAPS_PM_d3Ac_WT_RepBio4_Frac_05.raw	Raw
	20190423_SCX_ERACAPS_PM_d3Ac_WT_RepBio4_Frac_06.raw	Raw

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Publications

Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.

Bienvenut Willy V WV Brünje Annika A Boyer Jean-Baptiste JB Mühlenbeck Jens S JS Bernal Gautier G Lassowskat Ines I Dian Cyril C Linster Eric E Dinh Trinh V TV Koskela Minna M MM Jung Vincent V Seidel Julian J Schyrba Laura K LK Ivanauskaite Aiste A Eirich Jürgen J Hell Rüdiger R Schwarzer Dirk D Mulo Paula P Wirtz Markus M Meinnel Thierry T Giglione Carmela C Finkemeier Iris I

Molecular systems biology 20200701 7

Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All cha ...[more]

PMID: 32633465

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Project description:Acetylation of amino groups is an important and recurrent protein modification in all eukaryotes. In plants, both lysine and N-terminal acetylation have additional important roles in protein regulation in chloroplasts. However, it is yet unclear how acetylation patterns respond to environmental stresses, and whether lysine or N-terminal modifications similarly contribute to the associated perturbations. A new family of plastid acetyltransferase, called GNATs, was recently discovered, which consists of closely related enzymes featuring both lysine- and N-terminal acetyltransferase activities often on the same polypeptide targets. Here, we take advantage of this unique characteristic of Arabidopsis GNAT2 to obtain a holistic multi-omics acetylation-dependent view during the acclimation of plants to short term changes in light. No substantial difference in transcriptome or adenylate energy charge oscillations were observed between WT and gnat2 knockout mutant lines when they were submitted for two hours to high-light or dark growth conditions. A detailed characterization of the N-terminal acetylome reveals that both its yield and coverage remain unchanged upon different light conditions in both genotypes. Unlike the N-terminal acetylome, the GNAT2-associated lysine acetylome is sensitive to the different light conditions used. In addition, a strong reduction in both types of acetylations on several plastid proteins was observed upon GNAT2 inactivation under all light conditions. Our data suggests that the lysine acetylome marks on proteins more rapidly fluctuate following acclimation to the environmental condition, while N-terminal acetylation changes are associated to longer term responses, like those promoted in the gnat2 background. Taken together, our data revealed unique strategies of plant acclimation to the different applied treatments involving specific PTMs and emphasizes distinct timescale responses of plastid lysine and N-terminal acetylomes to environmental changes.