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N-terminal acetylation by NatB in Arabidopsis thaliana

ABSTRACT: N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. In this study, we investigated the Arabidopsis thaliana NatB catalytic (NAA20) and auxiliary subunit (NAA25) and their influence on protein N-terminal acetylation using the SILProNAQ approach

OTHER RELATED OMICS DATASETS IN: GSE132978

INSTRUMENT(S): LTQ Orbitrap

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

TISSUE(S): Leaf

SUBMITTER: Willy Bienvenut

LAB HEAD: Willy Vincent Bienvenut

PROVIDER: PXD016209 | Pride | 2019-11-21

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20140314_WIB_MAW_Naa20-1_Fracs-02-05-Ch1.dat	Other
	20140314_WIB_MAW_Naa20-1_Fracs-02-05-Ch1.mgf	Mgf
	20140314_WIB_MAW_Naa20-1_Fracs-02-05-Ch1.raw	Raw
	20140314_WIB_MAW_Naa20-1_Fracs-02-05-Ch2.dat	Other
	20140314_WIB_MAW_Naa20-1_Fracs-02-05-Ch2.mgf	Mgf

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Publications

NatB-Mediated N-Terminal Acetylation Affects Growth and Biotic Stress Responses.

Huber Monika M Bienvenut Willy V WV Linster Eric E Stephan Iwona I Armbruster Laura L Sticht Carsten C Layer Dominik D Lapouge Karine K Meinnel Thierry T Sinning Irmgard I Giglione Carmela C Hell Ruediger R Wirtz Markus M

Plant physiology 20191119 2

N<sup>∝</sup>-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes. In humans, NTA is catalyzed by seven N<sup>α</sup>-acetyltransferases (NatA-F and NatH). Remarkably, the plant Nat machinery and its biological relevance remain poorly understood, although NTA has gained recognition as a key regulator of crucial processes such as protein turnover, protein-protein interaction, and protein targeting. In this study, we combined in vitro assays, reverse genetics ...[more]

PMID: 31744933

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AtNAA50 N-terminal acetylation profiling using A. thaliana naa50 KO mutants

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plasma membrane anchored NAA60 N-terminal acetylation profiling in Arabidopsis thaliana

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Global acetylation profiling for multiple Arabidopsis thaliana plastid N-terminal acetyltransferases

Project description:Protein acetylation is a universally conserved modification occurring on N-termini (N-Terminal acetylation, NTA). Although recent reports indicate that NTA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylation and why these modifications are that frequent in this organelle. Searches for new putative N-acetyltransferase genes in Arabidopsis thaliana highlighted eight putative candidates located at plastid subcellular location. In this study, we investigated the N-acetyltransferase specificity of these enzymes using the global acetylome profiling test (GAP test).

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Global acetylation profiling for the Arabidopsis thaliana the N-acetyltransferase NAA50 in the NatA complex.

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Global acetylation profiling for the Arabidopsis thaliana plasma membrane anchored NAA60 N-terminal acetyltransferase

Project description:N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA60 is localized in vivo at the plasma membrane by an α-helical membrane anchor at its C-terminus. In this study, we investigated the Arabidopsis thaliana N-acetylome using the global acetylome profiling test (GAP test).

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Proteome imprinting by N-terminal acetylation is a vital hormone-regulated master switch during stress

Project description:N-terminal acetylation (NTA) catalyzed by N-terminal acetyltransferases (Nats) is among the most common protein modifications in eukaryotes, but its significance is still enigmatic. Characterization of the plant NatA complex reveals evolutionary conservation of NatA biochemical properties within higher eukaryotes and uncovers specific and essential functions of NatA for regulation of development, numerous biosynthetic pathways and stress responses in plants. We show that NTA decreases significantly in case of drought stress, since NatA abundance is rapidly down-regulated by the phytohormone abscisic acid. Accordingly, down-regulation of NatA by genetic engineering is sufficient for induction of the drought stress response and results in strikingly drought resistant plants. Thus, NTA by the NatA complex is a vital cellular surveillance mechanism during stress. We conclude that imprinting of the proteome by NatA is a master switch for control of metabolism, development and cellular stress responses and integrates stress signals by perceiving the hormone abscisic acid.

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Project description:Protein Nα-terminal acetylation represents one of the most abundant protein modifications of higher eukaryotes. In humans, six Nα-acetyltransferases (Nats) are responsible for the acetylation of approximately 80% of the cytosolic proteins. N-terminal protein acetylation has not been evidenced in organelles of metazoans, but in higher plants, it is a widespread modification not only in the cytosol but also in the chloroplast. In this study, we identify and characterize the first organellar-localized Nat in eukaryotes. A primary sequence-based search in Arabidopsis thaliana revealed seven putatively plastid-localized Nats of which AT2G39000 (AtNAA70) showed the highest conservation of the acetyl-CoA binding pocket. The chloroplastic localization of AtNAA70 was demonstrated by transient expression of AtNAA70:YFP in Arabidopsis mesophyll protoplasts. Homology modeling uncovered a significant conservation of tertiary structural elements between human HsNAA50 and AtNAA70. The in vivo acetylation activity of AtNAA70 was demonstrated on a number of distinct protein N alpha-termini with a newly established Nat-activity global profiling after expression of AtNAA70 in E. coli. AtNAA70 predominately acetylated proteins starting with M, A, S, and T, providing an explanation for most protein N-termini acetylation events found in chloroplasts.

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Proteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state

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Proteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition

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N-terminal acetylome analysis reveals an expanded substrate profile for the NatC N-terminal acetyltransferase complex in yeast

Project description:N-terminal acetylation is a conserved protein modification among eukaryotes, and the yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The enzymes responsible for the bulk of protein N-terminal acetylation in S. cerevisiae are the N-terminal acetyltransferases NatA, NatB and NatC. Thus far, proteome-wide identification of the in vivo protein substrates of yeast NatA and NatB has been performed by N-terminomics. Here, we used S. cerevisiae deleted for the NatC catalytic subunit Naa30 and identified 57 yeast NatC substrates by N-terminal combined fractional diagonal chromatography (COFRADIC) analysis. Interestingly, in addition to the canonical N-termini starting with ML, MI, MF and MW, yeast NatC substrates also included MY, MK, MM, MA, MV and MS. However, for some of these substrate types, such as MY, MK, MV and MS, we also uncovered (residual) non-NatC NAT activity, most likely due to the previously established redundancy between yeast NatC and NatE/Naa50. Thus, we have revealed a complex interplay between different NATs in targeting methionine-starting N-termini in yeast. Furthermore, our results showed that ectopic expression of human NAA30 rescued known NatC phenotypes in naa30∆ yeast, as well as partially restored the yeast NatC Nt-acetylome. Thus, we demonstrate an evolutionary conservation of NatC from yeast to human thereby underpinning future disease models to study pathogenic NAA30 variants. Overall, this work offers increased biochemical and functional insights into NatC-mediated N-terminal acetylation and provides a basis for future work to pinpoint the specific molecular mechanisms that link lack of NatC-mediated N-terminal acetylation to phenotypes of NatC deletion yeast

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