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

0536876 - MBÚ 2021 RIV US eng J - Journal Article
Bienvenut, W. - Bruenje, A. - Boyer, J-B. - Muehlenbeck, J. S. - Bernal, G. - Lassowskat, I. - Dian, C. - Linster, E. - Dinh, T. - Koskela, Minna M. - Jung, V. - Seidel, J. - Schyrba, L. K. - Ivanauskaite, A. - Eirich, J. - Hell, R. - Schwarzer, D. - Mulo, P. - Wirtz, M. - Meinnel, T. - Giglione, C. - Finkemeier, I.
Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.
Molecular Systems Biology. Roč. 16, č. 7 (2020), č. článku e9464. ISSN 1744-4292. E-ISSN 1744-4292
Institutional support: RVO:61388971
Keywords : acetylome * acetylome * co- and post-translational modifications * plastid * quantitative proteomics
OECD category: Biochemistry and molecular biology
Impact factor: 11.429, year: 2020
Method of publishing: Open access
https://www.embopress.org/doi/full/10.15252/msb.20209464

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.
Permanent Link: http://hdl.handle.net/11104/0314629