Dataset Information

Proteomic study of Naa20 inactivation in MEFs

ABSTRACT: This study focuses on the proteomic analysis of mouse embryonic fybroblasts where Naa20 can be inactivated, to observe its role in biological pathways and its effect on the N-terminal acetylation of proteins.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Mef Cell

SUBMITTER: Carmela Giglione

LAB HEAD: Carmela GIGLIONE

PROVIDER: PXD029641 | Pride | 2025-08-25

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20200624_SCX_RA_d3NAc_MEF_WT_RepBio1_10Fracs.xml	Xml
	20200624_SCX_RA_d3NAc_MEF_WT_RepBio1_Frac_02.raw	Raw
	20200624_SCX_RA_d3NAc_MEF_WT_RepBio1_Frac_03.raw	Raw
	20200624_SCX_RA_d3NAc_MEF_WT_RepBio1_Frac_04.raw	Raw
	20200624_SCX_RA_d3NAc_MEF_WT_RepBio1_Frac_05.raw	Raw

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Publications

NatB Protects Procaspase-8 from UBR4-Mediated Degradation and Is Required for Full Induction of the Extrinsic Apoptosis Pathway.

Guedes Joana P JP Boyer Jean Baptiste JB Elurbide Jasmine J Carte Beatriz B Redeker Virginie V Sago Laila L Meinnel Thierry T Côrte-Real Manuela M Giglione Carmela C Aldabe Rafael R

Molecular and cellular biology 20240804 9

N-terminal acetyltransferase B (NatB) is a major contributor to the N-terminal acetylome and is implicated in several key cellular processes including apoptosis and proteostasis. However, the molecular mechanisms linking NatB-mediated N-terminal acetylation to apoptosis and its relationship with protein homeostasis remain elusive. In this study, we generated mouse embryonic fibroblasts (MEFs) with an inactivated catalytic subunit of NatB (<i>Naa20</i><sup>-/-</sup>) to investigate the impact of ...[more]

PMID: 39099191

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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.