Archives of Microbiology

, Volume 114, Issue 1, pp 77–81 | Cite as

The formation of glycosidic bonds in yeast glycoproteins

Intracellular localisation of the reactions
  • L. Lehle
  • F. Bauer
  • W. Tanner


Membranes of Saccharomyces cerevisiae were separated on urografin gradients. The specific activity of the light membranes (endoplasmic reticulum), the Golgi-like vesicles and the plasma membrane in transferring mannosyl residues from GDP-mannose to mannoproteins and to dolichyl monophosphate has been determined. The first mannose of the O-glycosidically linked manno-oligosaccharides is incorporated with the highest specific activity by the endoplasmic reticulum. The incorporation of the second to fourth mannosyl groups is catalysed with increasing activity also by the Golgi-like vesicles and the plasma membrane.

The incorporation of mannosyl groups into weak alkali-stable positions (N-glycosidically linked chains) is carried out with almost the same specific activity by all three membrane fractions, however, dolicholdependent and-independent steps could not be distinguished as yet.

The results are discussed in terms of a sequential addition of sugar residues along the route of export of the mannoproteins. The dolichol-dependent steps seem to occur on the endoplasmic reticulum and thus very carly in the event.

Key words

Mannoproteins Dolichyl monophosphate mannose Subcellular site of glycosylation Secretion Saccharomyces cerevisiae 



guanosine diphosphate mannose


dolichyl monophosphate


dolichyl monophosphate mannose


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Copyright information

© Springer-Verlag 1977

Authors and Affiliations

  • L. Lehle
    • 1
  • F. Bauer
    • 1
  • W. Tanner
    • 1
  1. 1.Botanik I, Fachbereich Biologie und Vorklinische MedizinUniversität RegensburgRegensburgFederal Republic of Germany

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