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放线菌中蛋白质O-甘露糖基化的新见解。

New insights into protein O-mannosylation in actinomycetes.

作者信息

Espitia Clara, Servín-González Luis, Mancilla Raúl

机构信息

Departamento de Inmunologia, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, México DF, México.

出版信息

Mol Biosyst. 2010 May;6(5):775-81. doi: 10.1039/b916394h. Epub 2010 Feb 24.

Abstract

Glycosylation is a common post-translational modification of surface exposed proteins and lipids present in all kingdoms of life. Information derived from bacterial genome sequencing, together with proteomic and genomic analysis has allowed the identification of the enzymatic glycosylation machinery. Among prokaryotes, O-mannosylation of proteins has been found in the actinomycetes and resembles protein O-mannosylation in fungi and higher eukaryotes. In this review we summarize the main features of the biosynthetic pathway of O-mannosylation in prokaryotes with special emphasis on the actinomycetes, as well as the biological role of the glycosylated target proteins.

摘要

糖基化是一种常见的翻译后修饰,存在于所有生命王国的表面暴露蛋白和脂质中。来自细菌基因组测序的信息,以及蛋白质组学和基因组分析,使得酶促糖基化机制得以鉴定。在原核生物中,已在放线菌中发现蛋白质的O-甘露糖基化,且类似于真菌和高等真核生物中的蛋白质O-甘露糖基化。在本综述中,我们总结了原核生物中O-甘露糖基化生物合成途径的主要特征,特别强调放线菌,以及糖基化靶蛋白的生物学作用。

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