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

ABSTRACT: 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).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Escherichia Coli

SUBMITTER: Willy Bienvenut

LAB HEAD: Willy Bienvenut

PROVIDER: PXD016533 | Pride | 2020-07-15

REPOSITORIES: Pride

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The Arabidopsis N<sup>α</sup> -acetyltransferase NAA60 locates to the plasma membrane and is vital for the high salt stress response.

Linster Eric E Layer Dominik D Bienvenut Willy V WV Dinh Trinh V TV Weyer Felix A FA Leemhuis Wiebke W Brünje Annika A Hoffrichter Marion M Miklankova Pavlina P Kopp Jürgen J Lapouge Karine K Sindlinger Julia J Schwarzer Dirk D Meinnel Thierry T Finkemeier Iris I Giglione Carmela C Hell Ruediger R Sinning Irmgard I Wirtz Markus M

The New phytologist 20200716 2

In humans and plants, N-terminal acetylation plays a central role in protein homeostasis, affects 80% of proteins in the cytoplasm and is catalyzed by five ribosome-associated N-acetyltransferases (NatA-E). Humans also possess a Golgi-associated NatF (HsNAA60) that is essential for Golgi integrity. Remarkably, NAA60 is absent in fungi and has not been identified in plants. Here we identify and characterize the first plasma membrane-anchored post-translationally acting N-acetyltransferase AtNAA60 ...[more]

PMID: 32548857

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

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

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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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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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