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  Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein

Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., et al. (1992). Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein. Biological Chemistry Hoppe-Seyler., 373(4), 171-176.

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Peters, J.1, Author           
Rudolf, S., Author
Oschkinat, H.1, Author           
Mengele, R., Author
Sumper, M., Author
Kellermann, J.1, Author           
Lottspeich, F.1, Author           
Baumeister, W.1, Author           
Affiliations:
1External Organizations, ou_persistent22              

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Free keywords: Amino Acid Sequence; *Bacteria, Anaerobic/ch [Chemistry]; *Bacterial Outer Membrane Proteins/ch [Chemistry]; *Glycosaminoglycans/ch [Chemistry]; Molecular Sequence Data; Peptides/ch [Chemistry]; *Tyrosine/ch [Chemistry]
 Abstract: The S-layer protein of Acetogenium kivui was subjected to proteolysis with different proteases and several high molecular mass glycosaminoglycan peptides containing glucose, galactosamine and an unidentified sugar-related component were separated by molecular sieve chromatography and reversed-phase HPLC and subjected to N-terminal sequence analysis. By methylation analysis glucose was found to be uniformly 1,6-linked, whereas galactosamine was exclusively 1,4-linked. Hydrazinolysis and subsequent amino-acid analysis as well as two-dimensional NMR spectroscopy were used to demonstrate that in these peptides carbohydrate was covalently linked to tyrosine. As all of the four Tyr-glycosylation sites were found to be preceded by valine, a new recognition sequence for glycosylation is suggested.

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 Dates: 1992
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 318371
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Title: Biological Chemistry Hoppe-Seyler.
Source Genre: Journal
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Pages: - Volume / Issue: 373 (4) Sequence Number: - Start / End Page: 171 - 176 Identifier: -