Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation
Eric Linster; Vincent Jung; Paula Mulo; Minna M Koskela; Rüdiger Hell; Jens S Mühlenbeck; Jürgen Eirich; Cyril Dian; Ines Lassowskat; Iris Finkemeier; Gautier Bernal; Thierry Meinnel; Carmela Giglione; Trinh V Dinh; Julian Seidel; Aiste Ivanauskaite; Laura K Schyrba; Dirk Schwarzer; Jean‐Baptiste Boyer; Markus Wirtz; Willy V Bienvenut; Annika Brünje
Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation
Eric Linster
Vincent Jung
Paula Mulo
Minna M Koskela
Rüdiger Hell
Jens S Mühlenbeck
Jürgen Eirich
Cyril Dian
Ines Lassowskat
Iris Finkemeier
Gautier Bernal
Thierry Meinnel
Carmela Giglione
Trinh V Dinh
Julian Seidel
Aiste Ivanauskaite
Laura K Schyrba
Dirk Schwarzer
Jean‐Baptiste Boyer
Markus Wirtz
Willy V Bienvenut
Annika Brünje
WILEY
Julkaisun pysyvä osoite on:
https://urn.fi/URN:NBN:fi-fe2021042822559
https://urn.fi/URN:NBN:fi-fe2021042822559
Tiivistelmä
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.
Kokoelmat
- Rinnakkaistallenteet [19207]