Unit
UNIT 14.11 Analysis of Protein Lysine Acetylation In Vitro and In Vivo
Published Online: 1 NOV 2008
DOI: 10.1002/0471140864.ps1411s54
Copyright © 2008 by John Wiley & Sons, Inc.
Lab Protocol Title

Current Protocols in Protein Science
Additional Information
How to Cite
Pelletier, N., Grégoire, S. and Yang, X.-J. 2008. Analysis of Protein Lysine Acetylation In Vitro and In Vivo. Current Protocols in Protein Science. 54:14.11:14.11.1–14.11.17.
Publication History
- Published Online: 1 NOV 2008
- Published Print: NOV 2008
This is not the most recent version of the article. View current version (2 FEB 2017)
Abstract
Protein lysine acetylation, referring to acetylation of the ɛ-amino group of a lysine residue, has recently emerged as an important post-translational modification for regulating protein functions in various organisms. Like phosphorylation, lysine acetylation is a rapidly reversible and precisely controlled covalent modification that serves as a simple on/off switch or participates in a codified manner with other post-translational modifications to regulate protein functions in different cellular and developmental processes. This unit describes and discusses methods used for in vitro and in vivo determination of lysine acetylation. Curr. Protoc. Protein Sci. 54:14.11.1-14.11.17. © 2008 by John Wiley & Sons, Inc.
Keywords:
- lysine acetylation;
- histone acetylation;
- histone acetyltransferase;
- transcription;
- p53;
- tubulin;
- hsp90;
- chromatin
