Elleuche Skander, Döring Kristin, Pöggeler Stefanie
Institute of Microbiology and Genetics, Department of Genetics of Eukaryotic Microorganisms, Georg-August-University of Göttingen, Grisebachstrasse 8, 37077 Gottingen, Germany.
Biochem Biophys Res Commun. 2008 Feb 1;366(1):239-43. doi: 10.1016/j.bbrc.2007.11.126. Epub 2007 Dec 3.
Inteins are internal protein splicing elements that can autocatalytically self-excise from their host protein and ligate the protein flanks (exteins) with a peptide bond. Large inteins comprise independent protein splicing and endonuclease domains whereas mini-inteins lack the central endonuclease domain. To identify mini-intein domains that are essential for protein splicing, deletions were introduced at different sites of the 157-aa PRP8 mini-intein of Penicillium chrysogenum. The removal of eight and six amino acids at two different sites resulted in a functional eukaryotic mini-intein of only 143 aa.
内含肽是内部蛋白质剪接元件,能够从宿主蛋白中自动催化自我切除,并通过肽键连接蛋白质侧翼(外显肽)。大型内含肽包含独立的蛋白质剪接和内切核酸酶结构域,而小型内含肽则缺乏中央内切核酸酶结构域。为了鉴定蛋白质剪接所必需的小型内含肽结构域,在产黄青霉157个氨基酸的PRP8小型内含肽的不同位点引入了缺失。在两个不同位点去除八个和六个氨基酸后,产生了一个仅143个氨基酸的功能性真核小型内含肽。