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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
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
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
Histone H2B was mutated to give H2B^3-32. Total RNA from three replicate cultures of wild-type and mutant was isolated and the expression profiles were determined using Affymetrix arrays. Comparisons between the sample groups allow the identification of genes regulated by H2B N-terminal domain. Ex...
ORGANISM(S): Saccharomyces cerevisiae 
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
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 fre...
ORGANISM(S): Escherichia coli 
2020-07-13 | PXD016205 | Pride
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
Protein N-terminal proteoforms, which include both N-terminal modifications and sequence variation arising from processes such as proteolytic cleavage, are common in cells and have been reported to significantly impact protein stability. Systematically examining the correlation between these N-termi...
ORGANISM(S): Homo sapiens (Human) 
2025-08-21 | PXD057760 | Pride
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 th...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-07-15 | PXD016494 | Pride
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 Arabidopsis thaliana N-ter...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-07-15 | PXD017770 | Pride
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