Department of Medical Protein Research, VIB, Ghent, Belgium.
FEBS J. 2011 Oct;278(20):3822-34. doi: 10.1111/j.1742-4658.2011.08230.x. Epub 2011 Aug 2.
Cotranslational protein N-terminal modifications, including proteolytic maturation such as initiator methionine excision by methionine aminopeptidases and N-terminal blocking, occur universally. Protein alpha-N-acetylation, or the transfer of the acetyl moiety of acetyl-coenzyme A to nascent protein N-termini, catalysed by multisubunit N-terminal acetyltransferase complexes, generally takes place during protein translation. Nearly all protein modifications are known to influence different protein aspects such as folding, stability, activity and localization, and several studies have indicated similar functions for protein alpha-N-acetylation. However, until recently, protein alpha-N-acetylation remained poorly explored, mainly due to the absence of targeted proteomics technologies. The recent emergence of N-terminomics technologies that allow isolation of protein N-terminal peptides, together with proteogenomics efforts combining experimental and informational content have greatly boosted the field of alpha-N-acetylation. In this review, we report on such emerging technologies as well as on breakthroughs in our understanding of protein N-terminal biology.
共翻译蛋白 N 端修饰，包括蛋白原起始甲硫氨酸切除的蛋白水解成熟过程（如由氨肽酶进行的起始甲硫氨酸切除）和 N 端封闭，普遍存在。蛋白α-N-乙酰化，即乙酰辅酶 A 的乙酰部分转移到新生蛋白 N 端，由多亚基 N 端乙酰转移酶复合物催化，通常发生在蛋白翻译过程中。几乎所有的蛋白修饰都被认为会影响蛋白的不同方面，如折叠、稳定性、活性和定位，并且有几项研究表明蛋白α-N-乙酰化具有类似的功能。然而，直到最近，蛋白α-N-乙酰化仍然研究不足，主要是由于缺乏靶向蛋白质组学技术。最近出现的 N 端组学技术允许分离蛋白 N 端肽，以及结合实验和信息内容的蛋白质基因组学研究，极大地推动了α-N-乙酰化领域的发展。在这篇综述中，我们报告了这些新兴技术的进展以及我们对蛋白 N 端生物学的理解的突破。
