Abstract
The acetylation of the ε-amine of lysine residues has significant impacts on the cellular functions of proteins. Through the combination of unbiased and targeted analysis of acetylated proteins, biological insights on lysine acetylation are now routinely generated. To help in this endeavor, we describe detailed protocols for the identification of acetylated lysine residues and the preparation of multiple reagents for the characterization of these sites in order to obtain functional insights on this widespread modification.
Keywords:
HAT; KAT; LC-MS/MS; Lysine acetylation; TAP.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acetylation
-
Cell Line
-
Enzyme Assays
-
Histone Acetyltransferases / chemistry
-
Histone Acetyltransferases / metabolism
-
Humans
-
Lysine / chemistry
-
Lysine / metabolism*
-
Lysine Acetyltransferases / chemistry
-
Lysine Acetyltransferases / isolation & purification
-
Lysine Acetyltransferases / metabolism*
-
Mass Spectrometry
-
Peptides / chemistry
-
Peptides / metabolism
-
Protein Processing, Post-Translational
-
Recombinant Proteins
-
Yeasts / metabolism
Substances
-
Peptides
-
Recombinant Proteins
-
Lysine Acetyltransferases
-
Histone Acetyltransferases
-
Lysine