A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation
Tekijät: Willy V Bienvenut, Annika Brünje, Jean‐Baptiste Boyer, Jens S Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V Dinh, Minna M Koskela, Vincent Jung, Julian Seidel, Laura K Schyrba, Aiste Ivanauskaite, Jürgen Eirich, Rüdiger Hell, Dirk Schwarzer, Paula Mulo, Markus Wirtz, Thierry Meinnel, Carmela Giglione, Iris Finkemeier
Kustantaja: WILEY
Julkaisuvuosi: 2020
Journal: Molecular Systems Biology
Tietokannassa oleva lehden nimi: MOLECULAR SYSTEMS BIOLOGY
Lehden akronyymi: MOL SYST BIOL
Artikkelin numero: ARTN e9464
Vuosikerta: 16
Numero: 7
Sivujen määrä: 23
ISSN: 1744-4292
eISSN: 1744-4292
DOI: https://doi.org/10.15252/msb.20209464
Rinnakkaistallenteen osoite: https://research.utu.fi/converis/portal/detail/Publication/49057789
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes (NATs andKATs, respectively), although the possibility that the sameGCN5-relatedN-acetyltransferase (GNAT) can perform both functions has been debated. Here, we discovered a new family of plastid-localizedGNATs, which possess a dual specificity. All characterizedGNATfamily members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinctKAand relaxedNTAspecificities. Furthermore, inactivation ofGNAT2 leads to significantNTAorKAdecreases of several plastid proteins, while proteins of other compartments were unaffected. The data indicate that these enzymes have specific protein targets and likely display partly redundant selectivity, increasing the robustness of the acetylation processin vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryoticGNATs may also possess these previously underappreciated broader enzymatic activities.
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