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ProteomicsN-terminal acetylome analysis reveals an expanded substrate profile for the NatC N-terminal acetyltransferase complex in yeast
N-terminal acetylation is a conserved protein modification among eukaryotes, and the yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The enzymes responsible for the bulk of protein N-terminal acetylation in S. cerevisiae are the N-terminal acetyltransferases...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-26 | PXD039544 | Pride
Natc N-terminal acetylation N-alpha-acetyltransferase 30 (naa30) Saccharomyces cerevisiae N-terminal acetylome N-terminal cofradic N-terminomics. 
ProteomicsMetabolic regulation of N-terminal acetylation in yeast
N-terminal (Nt) acetylation, catalyzed by N-terminal acetyltransferases (NATs), has emerged as an important co-translational modification in eukaryotes, and involves the transfer of the acetyl moiety from acetyl-CoA (Ac-CoA) to the α-amino group of a nascent polypeptide. Here, we report the first gl...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-07 | PXD004326 | Pride
Metabolism Acetyl coenzyme a Saccharomyces cerevisiae N-terminal acetylation N-terminomics 
ProteomicsPositional proteomics reveals differences in N-terminal proteoform stability.
To understand the impact of alternative translation initiation on a proteome, we performed the first large-scale study of protein turnover rates in which we distinguish between N-terminal proteoforms pointing to translation initiation events. Using pulsed SILAC combined with N-terminal COFRADIC we m...
ORGANISM(S): Homo sapiens (Human) 
2013-03-14 | PXD002091 | Pride
Nt-acetylation Protein stability Alternative translation initiation Initiator methionine processing Protein turnover N-terminal proteoform Human N-terminal cofradic 
ProteomicsAn OMICS perspective on N-terminal Methionine Excision
Excision of the N-terminal initiator methionine (iMet) from nascent peptide chains is an essential and omnipresent protein modification carried out by Methionine aminopetidases (MetAPs) and accounting for a major source of N-terminal proteoform diversity. While MetAP2 is known to be implicated in pr...
ORGANISM(S): Homo sapiens (Human) 
2018-01-10 | PXD006638 | Pride
Metap Metap1 Shotgun N-terminal proteomics Imet excision 
ProteomicsChemical proteomics profiling of N-terminal and lysine acetyltransferases
Acetylation of amino groups is a prevalent protein modification in all kingdoms of life. Acetyl groups are transferred from Coenzyme A (CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA ...
ORGANISM(S): Homo Sapiens (human) 
2021-04-14 | PXD018544 | JPOST Repository
ProteomicsN-terminal acetylation by NatB in Arabidopsis thaliana
N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. In this study, we investigated the Arabidopsis thaliana NatB catalytic (NAA20) and auxiliary subunit (NAA25) and their influence on protein N-termina...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-11-21 | PXD016209 | Pride
Acetyltransferase N-acetylome N-terminal acetylation Quantitative proteomics Silpronaq Gap test 
ProteomicsN-terminal acetylome analyses reveals the substrate specificity profile of Naa50 (Nat5) and implicate NATs in influencing initiator Methionine processing
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 i...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-05-29 | PXD001437 | Pride
N-terminal acetyltransferase / n-terminomics / nt-acetylome / naa50 / nate 
ProteomicsDiscovering the N-terminal Methylome by the Repurposing of Proteomic Datasets
Protein ⍺-N-methylation is a cryptic and relatively unexplored post-translational modification involving the covalent addition of methyl groups to the free a-amino group at protein N-termini. To systematically explore the extent of ⍺-N-terminal methylation in yeast and humans, we utilized a repurpos...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-05-26 | PXD022833 | Pride
Proteomics Post-translational modification Repurposing ⍺-n-terminal methylation 
ProteomicsArabidopsis thaliana N-terminal proteome,LC-MS
An extended ChaFRADIC workflow was applied to analyze the N-terminal proteome of Arabidopsis thaliana seedlings. Using iTRAQ protein labeling, a multi-enzyme digestion approach including trypsin, GluC, and subtilisin, a total of 200 μg per enzyme were used, and only 1/3 of each ChaFRADIC-enriched fr...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2015-07-21 | PXD001855 | Pride
Arabidopsis thaliana Chafradic Itraq reagent Enrichment of n-terminal peptide 
ProteomicsSelective enrichment of N-terminal proline peptides via hydrazide chemistry for proteomics analysis
A challenge for shotgun proteomics is the identification of low abundance proteins, which is always hampered owing to the extreme complexity of protein digests and highly dynamic concentration range of proteins. To reduce the complexity of the peptide mixture, we developed a novel method to selectiv...
ORGANISM(S): Homo Sapiens 
2021-10-18 | PXD029178 |
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