N-glycosylation in Haloferax volcanii: adjusting the sweetness.
N-glycosylation in Haloferax volcanii: adjusting the sweetness.
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DOI：
10.3389/fmicb.2013.00403
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发表时间：
2013-12-24
影响因子：
5.2
通讯作者：
Konrad Z
中科院分区：
文献类型：
--
作者：
Eichler J;Arbiv A;Cohen-Rosenzweig C;Kaminski L;Kandiba L;Konrad Z
长期以来被认为仅限于真核生物，现在已知所有三个生命结构域的细胞都进行N-糖基化，即聚糖与选择的靶蛋白天冬酰胺残基的共价连接。尽管如此，它只是在过去的十年中，N-糖基化的途径，在大肠杆菌已经划定。在嗜盐古菌Haloferax volcanii中，一系列Agl（古菌糖基化）蛋白负责将N-连接的五糖添加到修饰的蛋白质，包括表面（S）层糖蛋白，其是围绕细胞的表面层的唯一组分。然而，S层糖蛋白N-连接的糖基化谱的变化，作为周围盐度的函数。在不同的盐浓度下生长时，S层糖蛋白或者被上面引入的N-连接的五糖修饰，或者被该五糖以及不同组成的四糖修饰。最近的努力已经将Agl 5-Agl 15鉴定为第二种Hfx的组分。volcanii N-糖基化途径，当生长发生在含1.75 M但不含3.4 M NaCl的培养基中时，该途径负责产生附着于S-层糖蛋白的四糖。
Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target protein asparagine residues. Still, it is only in the last decade that pathways of N-glycosylation in Archaea have been delineated. In the haloarchaeon Haloferax volcanii, a series of Agl (archaeal glycosylation) proteins is responsible for the addition of an N-linked pentasaccharide to modified proteins, including the surface (S)-layer glycoprotein, the sole component of the surface layer surrounding the cell. The S-layer glycoprotein N-linked glycosylation profile changes, however, as a function of surrounding salinity. Upon growth at different salt concentrations, the S-layer glycoprotein is either decorated by the N-linked pentasaccharide introduced above or by both this pentasaccharide as well as a tetrasaccharide of distinct composition. Recent efforts have identified Agl5–Agl15 as components of a second Hfx. volcanii N-glycosylation pathway responsible for generating the tetrasaccharide attached to S-layer glycoprotein when growth occurs in 1.75 M but not 3.4 M NaCl-containing medium.
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