Targeted large-scale analysis of protein acetylation.
Protein modifications are biologically important events that may be studied by mass spectrometry-based high-throughput proteome analyses. In recent years, several new technologies have emerged that have widened and deepened the targeted analysis of one important, albeit functionally ill-defined modification, namely protein acetylation. This modification can take place both co- and post-translationally by the transfer of acetyl groups under the catalysis of acetyltransferases. The acetyl group can modify either the α-amino group at the N-terminus, so-called N-terminal acetylation, or the ε-amino group on the side chain of lysine residues. Here, we review several emerging targeted technologies to chart both N-terminal acetylation as well as acetylation at the lysine side chain, on a proteome-wide scale, highlighting in particular studies that have expanded the biological knowledge on the appearance and function of these common but functionally still less investigated co- and post-translational modifications.
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan, CH Utrecht, The Netherlands.
Nikolai
N
Mischerikow
Albert J R
AJ
Heck
D000107:Acetylation; D000818:Animals; D002853:Chromatography, Liquid; D057166:High-Throughput Screening Assays / Q000379:methods*; D006801:Humans; D015336:Molecular Probe Techniques; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*
D011506:Proteins