Proteomics

Dataset Information

0

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


ABSTRACT: N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA50 interreact with the NatA complex (NAA10 and NAA15) to form the NatE complex. In this study, we investigated the activity of this catalytic subunit using the global acetylome profiling test (GAP test).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Escherichia Coli

SUBMITTER: Willy Bienvenut  

LAB HEAD: Willy Bienvenut

PROVIDER: PXD017767 | Pride | 2020-07-15

REPOSITORIES: Pride

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Publications

NAA50 Is an Enzymatically Active <i>N</i> <sup>α</sup>-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


N<sup>α</sup>-terminal acetylation (NTA) is a prevalent protein modification in eukaryotes. In plants, the biological function of NTA remains enigmatic. The dominant <i>N</i>-acetyltransferase (Nat) in Arabidopsis (<i>Arabidopsis thaliana</i>) 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 (<i>Homo sapiens</i>), fruit fly (<i>Drosophila melanogaster</i  ...[more]

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