Lysine Propionylation and Butyrylation Are Novel Post-translational Modifications in Histones
The University of Texas Southwestern Medical Center · Columbia University · +2 more institutions
Abstract
The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell physiology and pathology. Here we report the discovery of two novel, in vivo lysine modifications in histones, lysine propionylation and butyrylation. We confirmed, by in vitro labeling and peptide mapping by mass spectrometry, that two previously known acetyltransferases, p300 and CREB-binding protein, could catalyze lysine propionylation and lysine butyrylation in histones. Finally p300 and CREB-binding protein could carry out…
Citation impact
- FWCI
- 6.32
- Percentile
- 100%
- References
- 31
Authors
10- YCYue Chen
The University of Texas Southwestern Medical Center
- RWRobert W. Sprung
The University of Texas Southwestern Medical Center
- YTYi Tang
Columbia University, Cancer Genetics (United States)
- HLHaydn L. Ball
The University of Texas Southwestern Medical Center
- BSBhavani Sangras
The University of Texas Southwestern Medical Center
Topics & keywords
- Lysine
- Biochemistry
- Histone
- P300-CBP Transcription Factors
- CREB-binding protein
- Chemistry
- Acetylation
- Biology