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. 1986 Sep;83(17):6263–6266. doi: 10.1073/pnas.83.17.6263

Synthesis of an O-glycosylated cell surface protein induced in yeast by α factor

P Orlean 1,*, H Ammer 1, M Watzele 1, W Tanner 1,
PMCID: PMC386483  PMID: 16593749

Abstract

A number of cell surface glycoproteins can be specifically and completely released from intact cells of Saccharomyces cerevisiae with 0.5% mercaptoethanol. Among these proteins is one with a molecular mass of 22 kDa, which is synthesized only in haploid a cells treated with the peptide mating pheromone α factor. This protein could be radiolabeled in vivo with [2-3H]mannose, [14C]phenylalanine, and [35S]sulfate. Its synthesis and export to the cell surface were not inhibited by tunicamycin. β-Elimination released almost all radioactivity from the [2-3H]mannose-labeled protein, 36% of its radioactivity being recovered subsequently as mannose and 43% as a dimannoside. Evidence is presented that the 22-kDa O-glycosylated protein is a mating-type specific a cell agglutinin.

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Selected References

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