Institute of Biochemistry, University of Münster, Wilhelm-Klemm-Str. 2, 48149, Münster, Germany.
Cell Mol Life Sci. 2013 Apr;70(7):1185-206. doi: 10.1007/s00018-012-1120-4. Epub 2012 Aug 28.
Inteins catalyze a post-translational modification known as protein splicing, where the intein removes itself from a precursor protein and concomitantly ligates the flanking protein sequences with a peptide bond. Over the past two decades, inteins have risen from a peculiarity to a rich source of applications in biotechnology, biomedicine, and protein chemistry. In this review, we focus on developments of intein-related research spanning the last 5 years, including the three different splicing mechanisms and their molecular underpinnings, the directed evolution of inteins towards improved splicing in exogenous protein contexts, as well as novel applications of inteins for cell biology and protein engineering, which were made possible by a clearer understanding of the protein splicing mechanism.
内含子催化一种称为蛋白质剪接的翻译后修饰过程，其中内含子从前体蛋白中切除自身，并同时通过肽键连接侧翼的蛋白质序列。在过去的二十年中，内含子已经从一个奇特的现象变成了生物技术、生物医学和蛋白质化学中丰富的应用来源。在这篇综述中，我们重点介绍了过去 5 年内与内含子相关的研究进展，包括三种不同的剪接机制及其分子基础、内含子的定向进化以改善外源蛋白环境中的剪接效率，以及通过更清楚地了解蛋白质剪接机制而实现的内含子在细胞生物学和蛋白质工程中的新应用。
