Proteomics

Dataset Information

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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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Dataset's files

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Action DRS
20160722_WIB_Ctrl-GFP_Fracs-02-05_Ch1.dat Other
20160722_WIB_Ctrl-GFP_Fracs-02-05_Ch1.mgf Mgf
20160722_WIB_Ctrl-GFP_Fracs-02-05_Ch1.raw Raw
20160722_WIB_Ctrl-GFP_Fracs-02-05_Ch1_160729234056.dat Other
20160722_WIB_Ctrl-GFP_Fracs-02-05_Ch1_160729234056.mgf Mgf
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Publications

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]

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