Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan, CH Utrecht, The Netherlands.
Proteomics. 2011 Feb;11(4):571-89. doi: 10.1002/pmic.201000397. Epub 2011 Jan 18.
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.
蛋白质修饰是生物学上重要的事件，可以通过基于质谱的高通量蛋白质组学分析来研究。近年来，出现了几种新技术，拓宽并深化了对一种重要但功能尚未明确的修饰的靶向分析，即蛋白质乙酰化。这种修饰可以通过乙酰转移酶的催化，在翻译共和后转移乙酰基来发生。乙酰基可以修饰 N-末端的α-氨基，即所谓的 N 端乙酰化，或赖氨酸残基侧链上的ε-氨基。在这里，我们综述了几种新兴的靶向技术，以在蛋白质组范围内绘制 N 端乙酰化以及赖氨酸侧链上的乙酰化图谱，特别强调了那些扩展了对这些常见但功能研究较少的翻译共和后修饰的出现和功能的生物学知识的研究。
