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

• Published in: Molecular systems biology Vol. 16; no. 7; pp. e9464 - n/a
• Main Authors: Bienvenut, Willy V, Brünje, Annika, Boyer, Jean‐Baptiste, Mühlenbeck, Jens S, Bernal, Gautier, Lassowskat, Ines, Dian, Cyril, Linster, Eric, Dinh, Trinh V, Koskela, Minna M, Jung, Vincent, Seidel, Julian, Schyrba, Laura K, Ivanauskaite, Aiste, Eirich, Jürgen, Hell, Rüdiger, Schwarzer, Dirk, Mulo, Paula, Wirtz, Markus, Meinnel, Thierry, Giglione, Carmela, Finkemeier, Iris
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.07.2020; EMBO Press; John Wiley and Sons Inc; Springer Nature
• Subjects: Acetylation; acetylome; Acetyltransferase; Biochemistry, Molecular Biology; Cellular Biology; Chloroplasts; Complexity; co‐ and post‐translational modifications; Deactivation; EMBO30; EMBO31; EMBO56; Enzymatic activity; Enzymes; Genomes; Genomics; In vivo methods and tests; Inactivation; Life Sciences; Localization; Lysine; Mass spectrometry; Mass spectroscopy; Peptides; Phylogenetics; plastid; Plastids; Prokaryotes; Proteins; Quantitative Methods; quantitative proteomics; Selectivity; Structural Biology; Subcellular Processes; Vegetal Biology; co‐ and post‐translational modifications; plastid; acetylome; acetyltransferase; quantitative proteomics; Post-translational Modifications & Proteolysis; co-and post-translational modifications; Proteomics; quantitative proteomics Subject Categories Plant Biology

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 t...