Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles

• Published in: The Journal of biological chemistry Vol. 267; no. 12; pp. 8182 - 8185
• Main Authors: MENGELE, R, SUMPER, M
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 25.04.1992
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Bacterial Outer Membrane Proteins - isolation & purification; Bacterial Outer Membrane Proteins - metabolism; Biological and medical sciences; Carbohydrate Metabolism; Chromatography, High Pressure Liquid; comparison; Fundamental and applied biological sciences. Psychology; Gas Chromatography-Mass Spectrometry; Glycopeptides - isolation & purification; Glycopeptides - metabolism; Glycoproteins; Glycoproteins - metabolism; Glycosylation; Halobacterium - metabolism; Halobacterium salinarium; Haloferax volcanii; Molecular Sequence Data; Proteins; S-layer glycoproteins; stability; Trypsin - metabolism; Molecular structure; Archaeobacteria; Oligosaccharide; Bacteria; Halobacterium; Carbohydrate; Glycoproteins; Glycosylation; Halobacteriaceae; Comparative study; Sulfatation
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)42424-6

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.