MENGELE, R and SUMPER, M (1992) DRASTIC DIFFERENCES IN GLYCOSYLATION OF RELATED S-LAYER GLYCOPROTEINS FROM MODERATE AND EXTREME HALOPHILES. JOURNAL OF BIOLOGICAL CHEMISTRY, 267 (12). pp. 8182-8185. ISSN 0021-9258,
Full text not available from this repository.Abstract
The outer surface of the moderate halophilic archaebacterium Haloferax volcanii (formerly named Halobacterium volcanii) is covered with a hexagonally packed surface (S) layer glycoprotein. The polypeptide (794 amino acid residues) contains 7 N-glycosylation sites. Four of these sites were isolated as glycopeptides and the structure of one of the corresponding saccharides was determined. Oligosaccharides consisting of beta-1,4-linked glucose residues are attached to the protein via the linkage unit asparaginyl-glucose. In the related glycoprotein from the extreme halophile Halobacterium halobium, the glucose residues are replaced by sulfated glucuronic acid residues, causing a drastic increase in surface charge density. This is discussed in terms of a recent model explaining the stability of halophilic proteins.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HALOBACTERIUM-VOLCANII; METHYLATION ANALYSIS; BIOSYNTHESIS; PURIFICATION; PROTEIN; LINKAGE; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54568 |
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