Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea
Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea
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DOI：
10.1016/j.sbi.2008.06.010
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发表时间：
2008-10-01
影响因子：
6.8
通讯作者：
Sharon, Nathan
中科院分区：
文献类型：
--
作者：
Abu-Qarn, Mehtap;Eichler, Jerry;Sharon, Nathan
在蛋白质可以经历的许多翻译后修饰中，糖基化是最普遍和最多样化的。如今，很明显，曾经被认为仅限于真核生物的n -糖基化和o -糖基化也在细菌和古细菌中发生。的确，与真核生物相比，原核糖蛋白依赖于更多种类的单糖成分。近年来，在描述细菌和古细菌糖基化途径所涉及的酶方面取得了实质性进展。越来越清楚的是，增强对细菌糖基化酶的了解可能具有治疗价值，而将细菌糖基化基因引入大肠杆菌的能力表明糖工程向前迈出了一大步。更好地了解古菌蛋白糖基化，可以深入了解这种跨进化的翻译后修饰以及极端条件下的蛋白质加工。在这里，我们讨论与原核蛋白糖基化有关的新结构和生物合成发现，直到最近才被忽视的话题。
Of the many post-translational modifications proteins can undergo, glycosylation is the most prevalent and the most diverse. Today, it is clear that both N-glycosylation and O-glycosylation, once believed to be restricted to eukaryotes, also transpire in Bacteria and Archaea. Indeed, prokaryotic glycoproteins rely on a wider variety of monosaccharide constituents than do those of eukaryotes. In recent years, substantial progress in describing the enzymes involved in bacterial and archaeal glycosylation pathways has been made. It is becoming clear that enhanced knowledge of bacterial glycosylation enzymes may be of therapeutic value, while the demonstrated ability to introduce bacterial glycosylation genes into Escherichia coli represents a major step forward in glyco-engineering. A better understanding of archaeal protein glycosylation provides insight into this post-translational modification across evolution as well as protein processing under extreme conditions. Here, we discuss new structural and biosynthetic findings related to prokaryotic protein glycosylation, until recently a neglected topic.