Novel glycoproteins of the halophilic archaeon Haloferax volcanii

被引:21
作者
Eichler, J
机构
[1] Ben Gurion Univ Negev, Dept Life Sci, IL-84105 Beer Sheva, Israel
[2] Ben Gurion Univ Negev, Doris & Bertie Black Ctr Bioenerget Life Sci, IL-84105 Beer Sheva, Israel
基金
以色列科学基金会;
关键词
archaea; halophiles; Haloferax volcanii; glycoproteins; membranes; S-layer;
D O I
10.1007/s002030000152
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Archaea possess many eukaryote-like properties, including the ability to glycosylate proteins. Using oligosaccharide staining and lectin binding, this study revealed the existence of several glycosylated Haloferax volcanii membrane proteins, besides the previously reported surface layer (S-layer) glycoprotein. While the presence of glycoproteins in archaeal S-layers and flagella is well-documented, few archaeal glycoproteins that are not part of these structures have been reported. The glycosylated 150, 98, 58 and 54 kDa protein species detected were neither precursors nor breakdown products of the 190 kDa S-layer glycoprotein. Furthermore, these novel glycoproteins were outwardly oriented and intimately associated with the membrane.
引用
收藏
页码:445 / 448
页数:4
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