Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation - Archive ouverte HAL Access content directly
Journal Articles Molecular Systems Biology Year : 2020

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

Jens Mühlenbeck
  • Function : Author
Ines Lassowskat
  • Function : Author
Trinh Dinh
  • Function : Author
Minna Koskela
  • Function : Author
Julian Seidel
  • Function : Author
Laura Schyrba
  • Function : Author
Aiste Ivanauskaite
  • Function : Author
Jürgen Eirich
  • Function : Author
Rüdiger Hell
Dirk Schwarzer
Paula Mulo
  • Function : Author
Markus Wirtz

Abstract

Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N-a-acetylation (NTA) and e-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 characterized GNAT family members display a number of unique features. Quantitative mass spectrometry analyses revealed that these enzymes exhibit both distinct KA and relaxed NTA speci-ficities. Furthermore, inactivation of GNAT2 leads to significant NTA or KA decreases 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 process in vivo. In summary, this study revealed a new layer of complexity in the machinery controlling this prevalent modification and suggests that other eukaryotic GNATs may also possess these previously underappreciated broader enzy-matic activities.
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Dates and versions

hal-02988633 , version 1 (10-11-2020)

Licence

Attribution - CC BY 4.0

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Willy V. Bienvenut, Annika Brünje, Jean-Baptiste Boyer, Jens Mühlenbeck, Gautier Bernal, et al.. Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation. Molecular Systems Biology, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩. ⟨hal-02988633⟩
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