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原核生物中蛋白质糖基化的新角色

Sweet New Roles for Protein Glycosylation in Prokaryotes.

机构信息

Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.

Department of Biosciences, University of Oslo, 0316 Oslo, Norway.

出版信息

Trends Microbiol. 2017 Aug;25(8):662-672. doi: 10.1016/j.tim.2017.03.001. Epub 2017 Mar 21.

DOI:10.1016/j.tim.2017.03.001
PMID:28341406
Abstract

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.

摘要

长期以来,它被认为是真核生物所特有的一种翻译后修饰,但现在很清楚,细菌和古菌也能进行蛋白质糖基化,即将单糖到多糖共价连接到特定的蛋白质靶标上。与此同时,许多在真核生物中被赋予这种蛋白质加工事件的功能,如指导蛋白质折叠/质量控制、细胞内运输、决定细胞识别事件等,在原核生物中并不适用甚至无关。因此,蛋白质糖基化在细菌和古菌中必须具有新的功能。最近的研究工作已经开始阐明一些原核生物特有的功能,本文对此进行了综述。

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1
Sweet New Roles for Protein Glycosylation in Prokaryotes.原核生物中蛋白质糖基化的新角色
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Sweet to the extreme: protein glycosylation in Archaea.甜到极致:古菌中的蛋白质糖基化
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Glycoproteins in prokaryotes.原核生物中的糖蛋白。
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Prokaryotic ubiquitin-like protein modification.原核生物类泛素蛋白修饰
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Posttranslational protein modification in Archaea.古菌中的蛋白质翻译后修饰
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Protein glycosylation in Archaea: sweet and extreme.古菌中的蛋白质糖基化:甜蜜与极端并存。
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[Homologous protein domains in superkingdoms Archaea, Bacteria, and Eukaryota and the problem of the origin of eukaryotes].[古菌、细菌和真核生物超界中的同源蛋白质结构域以及真核生物起源问题]
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