Dataset Information

AtNAA50 behaviour in the core NatA complex

ABSTRACT: In eukaryotes, the N-terminal acetylation (NTA) is one of the most frequent protein modifications. In many organisms, and especially in plants, its biological function remains a mystery. In Arabidopsis thaliana, a large part of the proteome acetylation is catalyzed co-translationally by the action of the core NatA complex, which consitst of NAA10 and NAA15, respectively the catalytic and ribosome-anchoring subunits. This complex interacts with the NAA50 protein (NatE), which also has an N-acetyltransferase in organisms such as human and fruit fly. This project focuses on the effect of AtNAA50 knockouts on the activity of the essential NatA complex.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Leaf

SUBMITTER: Jean Baptiste BOYER

LAB HEAD: Carmela GIGLIONE

PROVIDER: PXD017430 | Pride | 2020-07-15

REPOSITORIES: Pride

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Publications

NAA50 Is an Enzymatically Active N α-Acetyltransferase That Is Crucial for Development and Regulation of Stress Responses.

Armbruster Laura L Linster Eric E Boyer Jean-Baptiste JB Brünje Annika A Eirich Jürgen J Stephan Iwona I Bienvenut Willy V WV Weidenhausen Jonas J Meinnel Thierry T Hell Ruediger R Sinning Irmgard I Finkemeier Iris I Giglione Carmela C Wirtz Markus M

Plant physiology 20200527 4

Nα-terminal acetylation (NTA) is a prevalent protein modification in eukaryotes. In plants, the biological function of NTA remains enigmatic. The dominant N-acetyltransferase (Nat) in Arabidopsis (Arabidopsis thaliana) is NatA, which cotranslationally catalyzes acetylation of ∼40% of the proteome. The core NatA complex consists of the catalytic subunit NAA10 and the ribosome-anchoring subunit NAA15. In human (Homo sapiens), fruit fly (Drosophila melanogaster</i ...[more]

PMID: 32461302

Similar Datasets

Project description:Co-translational N-terminal (Nt-) acetylation of nascent polypeptides is catalyzed by N-terminal acetyltransferases (NATs). The very N-terminal amino acid sequence is the major factor determining whether or not a given protein is Nt-acetylated. In humans, six different NATs, denoted NatA-NatF, are identified. In the current study we used N-terminal COFRADIC analysis to define the in vivo substrate specificity of Naa50 (Nat5)/NatE as this has long remained elusive. Three yeast strains were generated; a control strain endogenously expressing yNaa50, a deletion strain depleted of yNaa50 and a strain deleted of yNaa50 but ectopically expressing human Naa50. When comparing the Nt-acetylation status of different N-termini in the control strain with the deletion strain, a reduction in Nt-acetylation for several yeast proteins was observed. To our surprise, these substrates were not of the predicted NatE-type substrates, but rather canonical NatA substrates. Further, ectopic expression of hNaa50 mainly resulted in the Nt-acetylation of a selected class of otherwise Nt-free yeast N-termini besides increasing the degree of Nt-acetylation of several other yeast proteins, and as such (partially) complementing those N-termini displaying reduced Nt-acetylation upon yNAA50-deletion. The preferred substrates of hNaa50 were predominantly Met-starting N-termini including Met-Lys-, Met-Val-, Met-Ala-, Met-Tyr-, Met-Phe-, Met-Leu-, Met-Ser- and Met-Thr, and highly overlapped with the previously identified human Naa60/NatF substrate specificity profile. Identification of several hNaa50 substrates with a small amino acid in the second position also revealed a potential interplay between the NATs and methionine aminopeptidases (MetAPs). The initiator Methionine (iMet) is normally cleaved off by MetAPs when the second amino acid is small, but our in vitro data suggest that in contrast to a free iMet, an Nt-acetylated iMet is not hydrolyzed by MetAPs. Thus, Naa50-mediated Nt-acetylation may potentially act as a mechanism to retain the iMet of proteins with a small amino acid at the second position that normally would be hydrolyzed.

Dataset Information

AtNAA50 behaviour in the core NatA complex

Publications

NAA50 Is an Enzymatically Active <i>N</i> <sup>α</sup>-Acetyltransferase That Is Crucial for Development and Regulation of Stress Responses.

Similar Datasets

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