蛋白质内含子的研究进展

自1990年发现第一个蛋白质内含子以来,对其研究愈加引起注意。蛋白质内含子是蛋白质剪接元件,可从前体蛋白中切除并将两侧外显子连接起来成为成熟蛋白质,标准的蛋白质剪接主要包括四步亲核置换反应,新近又发现一种反式剪接机制。蛋白质内含子的演化形成存在先天遗传和后天插入两种方式,但目前还没有直接的实验证据。数据库显示,蛋白质内含子有10个保守模体：A、N2、B、N4、C、D、E、H、F和G,它们在蛋白质剪接过程中具有不同的作用。作为蛋白质剪切元件的蛋白质内含子,是蛋白质工程中一个功能强大的工具,具有重要的实践意义。现对蛋白质内含子的命名、分布、结构、剪接方式以及应用前景等作一全面的综述。

The disquisitive development about Intein

Since the first Intein was discovered in 1990, investigation about it was paid more and more attention. As a protein spli- cing element, it can be spliced from its precursor, and ligates the exons. There are four steps in the splicing of normal Inteins. Two fac- tors heredity and insertion play important roles in the evolvement of Intein, but experiment evidences haven＇ t been obtained up to now. According to the inBase, Intein included 10 conserved motifs： A, N2, B, N4, C, D, E, H, F and G. , they are all important to the Intein splicing process. Inteins are powerful tools in the protein project. They have significance in practice and can be used in many do- mains. There have been general research and analysis about its naming, distribution, structure, splicing mechanism and application foreground. The general review of Intein was made in the paper.