Dataset Information

N-terminal acetylation in Arabidopsis thaliana, and the effects of Naa10/15 or HypK knock-outs

ABSTRACT: This project is about the study of the effects of several proteins on the proteome of Arabidopsis thaliana, and more specifically on the N-terminal acetylome of this plant. To this end were analysed KO samples of either an N-alpha acetyltransferase (Naa10 or Naa15) or the chaperonne protein HypK.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Leaf

SUBMITTER: Jean Baptiste BOYER

LAB HEAD: Carmela GIGLIONE

PROVIDER: PXD023195 | Pride | 2022-08-12

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20170216_WIB_HypK1-Ech10.xml	Xml
	20170216_WIB_HypK1-Ech10_Frac02-05_Ch1.raw	Raw
	20170216_WIB_HypK1-Ech10_Frac02-05_Ch2.raw	Raw
	20170216_WIB_HypK1-Ech10_Frac02.raw	Raw
	20170216_WIB_HypK1-Ech10_Frac03.raw	Raw

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Publications

HYPK promotes the activity of the Nα-acetyltransferase A complex to determine proteostasis of nonAc-X2/N-degron-containing proteins.

Miklánková Pavlína P Linster Eric E Boyer Jean-Baptiste JB Weidenhausen Jonas J Mueller Johannes J Armbruster Laura L Lapouge Karine K De La Torre Carolina C Bienvenut Willy W Sticht Carsten C Mann Matthias M Meinnel Thierry T Sinning Irmgard I Giglione Carmela C Hell Rüdiger R Wirtz Markus M

Science advances 20220615 24

In humans, the Huntingtin yeast partner K (HYPK) binds to the ribosome-associated Nα-acetyltransferase A (NatA) complex that acetylates ~40% of the proteome in humans and Arabidopsis thaliana. However, the relevance of HsHYPK for determining the human N-acetylome is unclear. Here, we identify the AtHYPK protein as the first in vivo regulator of NatA activity in plants. AtHYPK physically interacts with the ribosome-anchoring subunit of NatA and promot ...[more]

PMID: 35704578

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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.

Dataset Information

N-terminal acetylation in Arabidopsis thaliana, and the effects of Naa10/15 or HypK knock-outs

Dataset's files

Publications

HYPK promotes the activity of the <i>N</i><sup>α</sup>-acetyltransferase A complex to determine proteostasis of nonAc-X<sup>2</sup>/N-degron-containing proteins.

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