Glycobiology, Vol 8, 1157-1164, Copyright © 1998 by Society for Glycobiology
R Zeitler, E Hochmuth, R Deutzmann and M Sumper
The archaeon Halobacterium halobium expresses a cell surface glycoprotein
(CSG) with a repeating pentasaccharide unit N- glycosidically linked via
N-acetylgalactosamine to Asn-2 of the polypeptide (GalNAc(1-N)Asn linkage
type). This aspar-agine of the linkage unit is located within the
N-terminal sequence Ala-Asn-Ala-Ser- , in accordance with the tripeptide
consensus sequence Asn-Xaa-Ser/Thr typical for nearly every N-glycosylation
site known so far, which are of the GlcNAc(1-N)-Asn linkage type. By a gene
replacement method csg mutants were created which replace the serine
residue of the consensus sequence by valine, leucine, and asparagine.
Unexpectedly, this elimination of the consensus sequence did not prevent
N-glycosylation. All respective mutant cell surface glycoproteins were
N-glycosylated at Asn-2 with the same N-glycan chain as the wild type CSG.
Asn-479 is N- glyco-sylated via a Glc(1-N)Asn linkage type in the wild type
CSG. Replacement of Ser-481 in the sequence Asn-Ser-Ser for valine
prevented glycosylation of Asn-479. From these results we postulate the
existence of two different N-glycosyltransferases in H.halobium, one of
which does not use the typical consensus sequence Asn-Xaa-Ser/Thr necessary
for all other N-glycosyltransferases described so far.
ORIGINAL ARTICLES
Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium
Lehrstuhl fur Biochemie I, Universitat Regensburg, Universit atsstrasse 31, 93040 Regensburg, Germany.
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