Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Curr Opin Chem Biol. 2018 Aug;45:1-9. doi: 10.1016/j.cbpa.2018.01.017. Epub 2018 Feb 22.
The genetic incorporation of unnatural amino acids (UAAs) into proteins by amber suppression technology provides unique avenues to study protein structure, function and interactions both in vitro and in living cells and organisms. This approach has been particularly useful for studying mechanisms of epigenetic chromatin regulation, since these extensively involve dynamic changes in structure, complex formation and posttranslational modifications that are difficult to access by traditional approaches. Here, we review recent achievements in this field, emphasizing UAAs that help to unravel protein-protein interactions in cells by photo-crosslinking or that allow the biosynthesis of proteins with defined posttranslational modifications for studying their function and turnover in vitro and in cells.
通过琥珀终止密码子抑制技术将非天然氨基酸(UAAs)掺入蛋白质中,为研究蛋白质的结构、功能和相互作用提供了独特的途径,无论是在体外还是在活细胞和生物体中。这种方法在研究表观遗传染色质调控机制方面特别有用,因为这些机制广泛涉及结构、复合物形成和翻译后修饰的动态变化,这些变化很难通过传统方法来实现。在这里,我们回顾了这一领域的最新进展,强调了通过光交联帮助揭示细胞中蛋白质-蛋白质相互作用的 UAAs,或者允许合成具有定义的翻译后修饰的蛋白质,以研究它们在体外和细胞中的功能和周转率。