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The plastidial protein acetyltransferase GNAT1 interacts with GNAT2 without affecting state transitions

ABSTRACT: The project focuses on the study of GCN5-related N-acetyltransferases (GNATs) in plants, which are plastidial proteins that possess dual lysine and N-terminal acetylation activities. More precisely, this study is based on the investigation of GNAT1, an uncharacterized member of the GNAT family, which catalytic domain has been observed to display similarities with that of the GNAT2 enzyme.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Rosette

SUBMITTER: Carmela Giglione

LAB HEAD: Dr Carmela GIGLIONE

PROVIDER: PXD046152 | Pride | 2024-08-19

REPOSITORIES: Pride

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			Action	DRS
	20201020_SCX_PM_d3NAc_Athliana_WT_RepBio1_10Fracs.rov	Other
	20201020_SCX_PM_d3NAc_Athliana_WT_RepBio1_10Fracs.xml	Xml
	20201020_SCX_PM_d3NAc_Athliana_WT_RepBio1_Frac_02.raw	Raw
	20201020_SCX_PM_d3NAc_Athliana_WT_RepBio1_Frac_02.rov	Other
	20201020_SCX_PM_d3NAc_Athliana_WT_RepBio1_Frac_03.raw	Raw

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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.

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The plastidial protein acetyltransferase GNAT1 interacts with GNAT2 without affecting state transitions

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