Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70
- PMID: 1551844
- PMCID: PMC205844
- DOI: 10.1128/jb.174.7.2236-2240.1992
Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70
Abstract
The surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70 was shown to contain a new type of glycan chain. Different from all known eubacterial glycoproteins, the saccharide moiety consists only of six sugar residues without any repeat sequences. Proteolytic digestion of purified S-layer glycoprotein resulted in isolation of several glycopeptide fractions. These are composed of the same hexasaccharide portion but are linked to oligopeptides of different length. One of them contains only a single amino acid. As concluded from chemical analyses and proton and carbon nuclear magnetic resonance spectroscopy of this preparation, the hexasaccharide moiety is linked via a novel O-glycosidic linkage. This is a beta-D-glucose residue linked to the phenolic hydroxyl group of tyrosine in intact S-layer glycoprotein.
Similar articles
-
Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70.J Bacteriol. 1993 Mar;175(5):1250-6. doi: 10.1128/jb.175.5.1250-1256.1993. J Bacteriol. 1993. PMID: 8444787 Free PMC article.
-
Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricum L77-66.Biochim Biophys Acta. 1992 Jul 21;1117(1):71-7. doi: 10.1016/0304-4165(92)90164-p. Biochim Biophys Acta. 1992. PMID: 1320936
-
Isolation and characterization of an amino sugar-rich glycopeptide from the surface layer glycoprotein of Thermoanaerobacterium thermosaccharolyticum E207-71.Carbohydr Res. 1996 Dec 13;295:245-53. doi: 10.1016/s0008-6215(96)90150-0. Carbohydr Res. 1996. PMID: 9002194 No abstract available.
-
Effect of N-linked glycosylation on glycopeptide and glycoprotein structure.Curr Opin Chem Biol. 1999 Dec;3(6):643-9. doi: 10.1016/s1367-5931(99)00021-6. Curr Opin Chem Biol. 1999. PMID: 10600722 Review.
-
Methods in enzymology: O-glycosylation of proteins.Methods Enzymol. 2005;405:139-71. doi: 10.1016/S0076-6879(05)05007-X. Methods Enzymol. 2005. PMID: 16413314 Review.
Cited by
-
A glycoprotein multimer from Bacillus thuringiensis sporangia: dissociation into subunits and sugar composition.Mol Cell Biochem. 1995 Apr 12;145(1):29-37. doi: 10.1007/BF00925710. Mol Cell Biochem. 1995. PMID: 7659076
-
Protein tyrosine O-glycosylation--a rather unexplored prokaryotic glycosylation system.Glycobiology. 2010 Jun;20(6):787-98. doi: 10.1093/glycob/cwq035. Epub 2010 Mar 3. Glycobiology. 2010. PMID: 20200052 Free PMC article.
-
Regulation and Characterization of Xylanolytic Enzymes of Thermoanaerobacterium saccharolyticum B6A-RI.Appl Environ Microbiol. 1993 Mar;59(3):763-71. doi: 10.1128/aem.59.3.763-771.1993. Appl Environ Microbiol. 1993. PMID: 16348890 Free PMC article.
-
Emerging facets of prokaryotic glycosylation.FEMS Microbiol Rev. 2017 Jan;41(1):49-91. doi: 10.1093/femsre/fuw036. Epub 2016 Aug 26. FEMS Microbiol Rev. 2017. PMID: 27566466 Free PMC article. Review.
-
Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.Infect Immun. 1999 Aug;67(8):3816-23. doi: 10.1128/IAI.67.8.3816-3823.1999. Infect Immun. 1999. PMID: 10417143 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials