Bobeica Silvia C, van der Donk Wilfred A
Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL, United States.
Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL, United States.
Methods Enzymol. 2018;604:165-203. doi: 10.1016/bs.mie.2018.01.038. Epub 2018 Mar 12.
Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides containing thioether cross-links formed through addition of a cysteine to a dehydroalanine (to form lanthionine) or to a dehydrobutyrine (to form 3-methyllanthionine). Genome sequencing of marine cyanobacteria lead to the discovery of 1.6 million open reading frames encoding lanthipeptides. In many cases, a genome encodes a single lanthipeptide synthetase, but a large number of substrates. The enzymatic modification process in Prochlorococcus MIT9313 has been reconstituted in vitro, and a variety of experimental approaches have been used to try and understand how one enzyme is capable of modifying 30 different substrates. The methods used to characterize this system will be described along with a brief genomic description of the lanthipeptide landscape found in Prochlorococcus and Synechococcus.
羊毛硫肽是核糖体合成并经翻译后修饰的肽，含有通过半胱氨酸添加到脱氢丙氨酸（形成羊毛硫氨酸）或脱氢丁氨酸（形成3-甲基羊毛硫氨酸）而形成的硫醚交联。海洋蓝细菌的基因组测序导致发现了160万个编码羊毛硫肽的开放阅读框。在许多情况下，一个基因组编码一种羊毛硫肽合成酶，但有大量底物。嗜球藻属MIT9313中的酶促修饰过程已在体外重建，并且已经使用了各种实验方法来尝试理解一种酶如何能够修饰30种不同的底物。将描述用于表征该系统的方法以及对嗜球藻属和聚球藻属中发现的羊毛硫肽概况的简要基因组描述。
