Abstract
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.
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Abbreviations
- GDP-mannose:
-
guanosine diphosphate mannose
- Dol-P:
-
dolichyl monophosphate
- Dol-P-mannose:
-
dolichyl monophosphate mannose
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Lehle, L., Bauer, F. & Tanner, W. The formation of glycosidic bonds in yeast glycoproteins. Arch. Microbiol. 114, 77–81 (1977). https://doi.org/10.1007/BF00429634
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DOI: https://doi.org/10.1007/BF00429634