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Proc Natl Acad Sci U S A

Title:		Synthesis of an O-glycosylated cell surface protein induced in yeast by alpha factor
Author(s):		Orlean P; Ammer H; Watzele M; Tanner W;
Address:		"Institut fur Botanik der Universitat Regensburg, Universitatsstrasse 31, 8400 Regensburg, Federal Republic of Germany"
Journal Title:		Proc Natl Acad Sci U S A
Year:		1986
Volume:		83
Issue:		17
Page Number:		6263 - 6266
DOI:		10.1073/pnas.83.17.6263
ISSN/ISBN:		0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
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 alpha factor. This protein could be radiolabeled in vivo with [2-(3)H]mannose, [(14)C]phenylalanine, and [(35)S]sulfate. Its synthesis and export to the cell surface were not inhibited by tunicamycin. beta-Elimination released almost all radioactivity from the [2-(3)H]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"
Keywords:
Notes:		"PubMed-not-MEDLINEOrlean, P Ammer, H Watzele, M Tanner, W eng 1986/09/01 Proc Natl Acad Sci U S A. 1986 Sep; 83(17):6263-6. doi: 10.1073/pnas.83.17.6263"