4.4 Article

Add salt, add sugar: N-glycosylation in Haloferax volcanii

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 41, 期 -, 页码 432-435

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST20120142

关键词

Archaea; Haloferax volcanii; N-glycosylation; post-translational modification; proteomic diversity

资金

  1. Israel Science Foundation [8/11]
  2. US Army Research Office [W911NF-11-1-520]
  3. Negev-Zin Associates Scholarship

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.4
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据