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Molecular & Cellular Proteomics 8:45-52, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Molecular Characterization of Propionyllysines in Non-histone Proteins ^*,S

Zhongyi Cheng^,,¶, Yi Tang^,||, Yue Chen, Sungchan Kim^**, Huadong Liu, Shawn S.C. Li, Wei Gu^||, and Yingming Zhao^,¶,¶¶

From the Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, ^|| Institute for Cancer Genetics, College of Physicians and Surgeons, Columbia University, New York, New York 10032, ^** Department of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-Do, 200-702, Korea, and the Department of Biochemistry and the Siebens-Drake Research Institute, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario N6A 5CI, Canada

Lysine propionylation and butyrylation are protein modifications that were recently identified in histones. The molecular components involved in the two protein modification pathways are unknown, hindering further functional studies. Here we report identification of the first three in vivo non-histone protein substrates of lysine propionylation in eukaryotic cells: p53, p300, and CREB-binding protein. We used mass spectrometry to map lysine propionylation sites within these three proteins. We also identified the first two in vivo eukaryotic lysine propionyltransferases, p300 and CREB-binding protein, and the first eukaryotic depropionylase, Sirt1. p300 was able to perform autopropionylation on lysine residues in cells. Our results suggest that lysine propionylation, like lysine acetylation, is a dynamic and regulatory post-translational modification. Based on these observations, it appears that some enzymes are common to the lysine propionylation and lysine acetylation regulatory pathways. Our studies therefore identified first several important players in lysine propionylation pathway.

^¶¶ To whom correspondence may be addressed. E-mail: Yingming.Zhao{at}uchicago.edu

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