Unit

UNIT 14.11 Analysis of Protein Lysine Acetylation In Vitro and In Vivo

  1. Nadine Pelletier,
  2. Serge Grégoire,
  3. Xiang-Jiao Yang

Published Online: 1 NOV 2008

DOI: 10.1002/0471140864.ps1411s54

Current Protocols in Protein Science

Current Protocols in Protein Science

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.

Author Information

  1. Rosalind and Morris Goodman Cancer Center and Department of Medicine, McGill University, Montreal, Canada

Publication History

  1. Published Online: 1 NOV 2008
  2. Published Print: NOV 2008

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