PXD040235

PXD040235 is an original dataset announced via ProteomeXchange.

Title	Light availability promotes distinct responses of plastid protein acetylation marks directed from the N-acetyltransferase GNAT2
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.
HostingRepository	PRIDE
AnnounceDate	2024-09-13
AnnouncementXML	Submission_2024-09-13_10:11:24.206.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Carmela Giglione
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-17 06:50:55	ID requested
⏵ 1	2024-09-13 10:11:24	announced

Dataset with its publication pending

submitter keyword: gnat2, acetylation,Arabidopsis, light, thaliana, acetylome, proteomics, acetyltransferase, light acclimation, NTA, quantitative, plastid, co- and post-translational modifications

Carmela GIGLIONE
contact affiliation	Protein Maturation, Cell fate and Therapeutics, Institute for Integrative Biology of the Cell (I2BC), CNRS UMR9198, Batiment 21, 1 Avenue de la Terrasse F-91198 Gif-sur-Yvette CEDEX, France
contact email	carmela.giglione@i2bc.paris-saclay.fr
lab head
Carmela Giglione
contact affiliation	CNRS
contact email	carmela.giglione@i2bc.paris-saclay.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD040235
     1. Label: PRIDE project
     2. Name: Light availability promotes distinct responses of plastid protein acetylation marks directed from the N-acetyltransferase GNAT2