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Originally published in Science Express on 16 July 2009
Science 14 August 2009:
Vol. 325. no. 5942, pp. 834 - 840
DOI: 10.1126/science.1175371
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Research Articles

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

Chunaram Choudhary,1,2 Chanchal Kumar,1 Florian Gnad,1 Michael L. Nielsen,1,2 Michael Rehman,3 Tobias C. Walther,3 Jesper V. Olsen,1,2 Matthias Mann1,2,*

Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation’s cellular roles. We used high-resolution mass spectrometry to identify 3600 lysine acetylation sites on 1750 proteins and quantified acetylation changes in response to the deacetylase inhibitors suberoylanilide hydroxamic acid and MS-275. Lysine acetylation preferentially targets large macromolecular complexes involved in diverse cellular processes, such as chromatin remodeling, cell cycle, splicing, nuclear transport, and actin nucleation. Acetylation impaired phosphorylation-dependent interactions of 14-3-3 and regulated the yeast cyclin-dependent kinase Cdc28. Our data demonstrate that the regulatory scope of lysine acetylation is broad and comparable with that of other major posttranslational modifications.

1 Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
2 The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen, Denmark.
3 Organelle Architecture and Dynamics, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.

* To whom correspondence should be addressed. E-mail: mmann{at}biochem.mpg.de

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