Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

Bogi Karbech Hansen, Rajat Gupta, Linda Baldus, David Lyon, Takeo Narita, Michael Lammers, Chunaram Choudhary () and Brian T. Weinert ()
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Bogi Karbech Hansen: University of Copenhagen
Rajat Gupta: University of Copenhagen
Linda Baldus: University of Greifswald
David Lyon: University of Copenhagen
Takeo Narita: University of Copenhagen
Michael Lammers: University of Greifswald
Chunaram Choudhary: University of Copenhagen
Brian T. Weinert: University of Copenhagen

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6829 sites on 2535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation (>1%) occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy numbers show that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation. This resource dataset provides valuable information for evaluating the impact of individual acetylation sites on protein function and for building accurate mechanistic models.

Date: 2019
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DOI: 10.1038/s41467-019-09024-0

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