Molecular identification and functional characterization of the first Nα-acetyltransferase in plastids by global acetylome profiling.

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In humans, six N(α) -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 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(α) -termini with a newly established global acetylome profiling test 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. Like HsNAA50, AtNAA70 displays N(ε) -acetyltransferase activity on three internal lysine residues. All MS data have been deposited in the ProteomeXchange with identifier PXD001947 (http://proteomecentral.proteomexchange.org/dataset/PXD001947).", "claims": [{"id": "claim-data-access", "statement": "The MS proteomics data in this paper have been deposited in the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [46]: dataset identifier PXD001947.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:25951519", "locator": "sections[20] \"ack\" paragraph 1", "quote": "The MS proteomics data in this paper have been deposited in the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository [46]: dataset identifier PXD001947."}], "state": "complete"}, {"id": "claim-target-result", "statement": "The paper used a global acetylome profiling (GAP) approach to test Nα-acetyltransferase activity; the source MS data were deposited in ProteomeXchange under identifier PXD001947. 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