Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
Biochem Soc Trans. 2013 Feb 1;41(1):432-5. doi: 10.1042/BST20120142.
Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii have, however, begun to correct this situation. A combination of bioinformatics, molecular biology, biochemical and mass spectrometry approaches have served to delineate the Agl pathway responsible for N-glycosylation of the S-layer glycoprotein, a reporter of this post-translational modification in Hfx. volcanii. More recently, differential N-glycosylation of the S-layer glycoprotein as a function of environmental salinity was demonstrated, showing that this post-translational modification serves an adaptive role in Hfx. volcanii. Furthermore, manipulation of the Agl pathway, together with the capability of Hfx. volcanii to N-glycosylate non-native proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.
尽管所有三个生命领域的成员都能进行 N-糖基化，但古菌版本的 N-糖基化仍然是了解最少的。然而，对火球菌的研究已经开始纠正这种情况。生物信息学、分子生物学、生物化学和质谱分析方法的结合，已经确定了负责 S 层糖蛋白 N-糖基化的 Agl 途径，该糖蛋白是 Hfx. volcanii 中这种翻译后修饰的报告蛋白。最近，还证明了 S 层糖蛋白的差异 N-糖基化是环境盐度的功能，表明这种翻译后修饰在火球菌中起着适应性作用。此外，Agl 途径的操纵，以及火球菌 N-糖基化非天然蛋白质的能力，为将该物种建立为糖工程平台奠定了基础。在本综述中，讨论了这些和其他最近的发现。
