Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein.
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.
Peters
J
J
Max-Planck-Institut für Biochemie, Martinsried bei München.
Rudolf
S
S
Oschkinat
H
H
Mengele
R
R
Sumper
M
M
Kellermann
J
J
Lottspeich
F
F
Baumeister
W
W
D000595:Amino Acid Sequence; D001421:Bacteria, Anaerobic / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001426:Bacterial Proteins; D006025:Glycosaminoglycans / Q000737:chemistry*; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D006025:Glycosaminoglycans; D008562:Membrane Glycoproteins; D010455:Peptides; C055764:S-layer proteins; D014443:Tyrosine