Proteomics

Dataset Information

0

Global acetylation profiling for multiple Arabidopsis thaliana plastid N-terminal acetyltransferases


ABSTRACT: Protein acetylation is a universally conserved modification occurring on N-termini (N-Terminal acetylation, NTA). Although recent reports indicate that NTA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylation and why these modifications are that frequent in this organelle. Searches for new putative N-acetyltransferase genes in Arabidopsis thaliana highlighted eight putative candidates located at plastid subcellular location. In this study, we investigated the N-acetyltransferase specificity of these enzymes using the global acetylome profiling test (GAP test).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Escherichia Coli

SUBMITTER: Willy Bienvenut  

LAB HEAD: Willy Bienvenut

PROVIDER: PXD016205 | Pride | 2020-07-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20121114_WIB_GNAT4_Frac2-5_ch1.dat Other
20121114_WIB_GNAT4_Frac2-5_ch1.mgf Mgf
20121114_WIB_GNAT4_Frac2-5_ch1.raw Raw
20121114_WIB_GNAT4_Frac2-5_ch2.dat Other
20121114_WIB_GNAT4_Frac2-5_ch2.mgf Mgf
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Publications


Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-α-acetylation (NTA) and ε-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs and KATs, respectively), although the possibility that the same GCN5-related N-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localized GNATs, which possess a dual specificity. All cha  ...[more]

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