Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap
ORGANISM(S): Escherichia Coli
SUBMITTER: Willy Bienvenut
LAB HEAD: Willy Bienvenut
PROVIDER: PXD016205 | Pride | 2020-07-13
REPOSITORIES: Pride
Bienvenut Willy V WV Brünje Annika A Boyer Jean-Baptiste JB Mühlenbeck Jens S JS Bernal Gautier G Lassowskat Ines I Dian Cyril C Linster Eric E Dinh Trinh V TV Koskela Minna M MM Jung Vincent V Seidel Julian J Schyrba Laura K LK Ivanauskaite Aiste A Eirich Jürgen J Hell Rüdiger R Schwarzer Dirk D Mulo Paula P Wirtz Markus M Meinnel Thierry T Giglione Carmela C Finkemeier Iris I
Molecular systems biology 20200701 7
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]