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Sweet New Roles for Protein Glycosylation in Prokaryotes
Trends in Microbiology ( IF 15.9 ) Pub Date : 2017-03-21 , DOI: 10.1016/j.tim.2017.03.001
Jerry Eichler , Michael Koomey

Long-held to be a post-translational modification unique to Eukarya, it is now clear that both Bacteria and Archaea also perform protein glycosylation, namely the covalent attachment of mono- to polysaccharides to specific protein targets. At the same time, many of the roles assigned to this protein-processing event in eukaryotes, such as guiding protein folding/quality control, intracellular trafficking, dictating cellular recognition events and others, do not apply or are even irrelevant to prokaryotes. As such, protein glycosylation must serve novel functions in Bacteria and Archaea. Recent efforts have begun to elucidate some of these prokaryote-specific roles, which are addressed in this review.



中文翻译:

在原核生物中蛋白质糖基化的甜新作用。

长期以来,它一直是Eukarya特有的翻译后修饰,现在很清楚,细菌和古生菌也都执行蛋白质糖基化作用,即单糖与多糖共价连接到特定的蛋白质靶标上。同时,在真核生物中赋予该蛋白质加工事件的许多作用,例如指导蛋白质折叠/质量控制,细胞内运输,指示细胞识别事件等,均不适用,甚至与原核生物无关。因此,蛋白质糖基化必须在细菌和古细菌中发挥新功能。最近的努力已经开始阐明这些原核生物特有的作用,本综述对此进行了讨论。

更新日期:2017-03-21
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