Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes.

Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes.
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DOI:
10.1155/2010/148178
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发表时间:
2010
影响因子:
3.4
通讯作者:
Hitchen P
Hitchen P
中科院分区:
其他
文献类型:
--
作者:
Dell A;Galadari A;Sastre F;Hitchen P

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近年来,已经见证了携带N-和/或O-聚糖的原核蛋白质的数量和多样性的快速增长,蛋白质糖基化现在被认为是这些生物体的生物学的基础,因为它是在真核系统中。本文综述了已知存在于真核生物、细菌和古细菌中的主要糖基化途径。这些是(i)寡糖基转移酶(OST)介导的N-糖基化,其在真核生物和古细菌中丰富,但限于有限范围的细菌;(ii)逐步的细胞质N-糖基化,其迄今为止仅在细菌结构域中被证实;(iii)OST介导的O-糖基化,其似乎是细菌的特征;和(iv)逐步的O-糖基化,其在真核生物和细菌中常见。综述的一个主要目的是整合来自生命三个领域的信息,以突出糖基化过程中的共性。我们展示了OST介导的N-和O-糖基化途径如何共享脂联寡糖的细胞质组装,翻转穿过ER/周质膜/细胞质膜,并将“整块”转移到蛋白质受体。此外,这些特征反映在脂多糖生物合成中。与真核生物一样,在包括鞭毛蛋白、粘附素、自身转运蛋白和脂蛋白在内的多种细菌蛋白上发生逐步O-糖基化,O-糖基化链延伸通常与分泌机制相结合。
Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems. This article overviews the major glycosylation pathways that are known to exist in eukarya, bacteria and archaea. These are (i) oligosaccharyltransferase (OST)-mediated N-glycosylation which is abundant in eukarya and archaea, but is restricted to a limited range of bacteria; (ii) stepwise cytoplasmic N-glycosylation that has so far only been confirmed in the bacterial domain; (iii) OST-mediated O-glycosylation which appears to be characteristic of bacteria; and (iv) stepwise O-glycosylation which is common in eukarya and bacteria. A key aim of the review is to integrate information from the three domains of life in order to highlight commonalities in glycosylation processes. We show how the OST-mediated N- and O-glycosylation pathways share cytoplasmic assembly of lipid-linked oligosaccharides, flipping across the ER/periplasmic/cytoplasmic membranes, and transferring “en bloc” to the protein acceptor. Moreover these hallmarks are mirrored in lipopolysaccharide biosynthesis. Like in eukaryotes, stepwise O-glycosylation occurs on diverse bacterial proteins including flagellins, adhesins, autotransporters and lipoproteins, with O-glycosylation chain extension often coupled with secretory mechanisms.