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Arabidopsis thaliana N-terminal Acetylome

ABSTRACT: Quantitative study of the N-terminal acetylome variations in Arabidopsis thaliana, looking at the effect of a N-acetyltransferase KO.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Rosette

SUBMITTER: Jean Baptiste BOYER

LAB HEAD: Carmela GIGLIONE

PROVIDER: PXD016496 | Pride | 2020-07-13

REPOSITORIES: Pride

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Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.

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]

PMID: 32633465

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