Proteomics

Dataset Information

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

ABSTRACT: N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. AtNAA60 localizes to the plasma membrane in vivo by an α-helical membrane anchor at its C-terminus. In this study, we investigated the Arabidopsis thaliana N-terminal acetylome in leaf cells of naa60-1 to identify AtNAA60 substrates in vivo using the SILProNAQ approach.

INSTRUMENT(S): LTQ Orbitrap

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

TISSUE(S): Leaf

SUBMITTER: Willy Bienvenut  

LAB HEAD: Willy Bienvenut

PROVIDER: PXD016494 | Pride | 2020-07-15

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20170210_WIB_DNaa60-Ech05_Frac02-05_Ch1-R.dat Other
20170210_WIB_DNaa60-Ech05_Frac02-05_Ch1-R.mgf Mgf
20170210_WIB_DNaa60-Ech05_Frac02-05_Ch1-R.raw Raw
20170210_WIB_DNaa60-Ech05_Frac02-05_Ch1.dat Other
20170210_WIB_DNaa60-Ech05_Frac02-05_Ch1.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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