Heleen, L. Caro, P. Tettelin, H. Vossen, J.H. Ram, A.F.J. Van Den Ende, H. Klis, F.M. text xx 9999 monographic und

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Use of the Von Heijne algorithm allowed the identification of 686 open reading frames (ORFs)in the genome of Saccharomyces cerevisiae that encode proteins with a potential N-terminal signal sequence for entering the secretory pathway. On further analysis, 51 of these proteins contain a potential glycosyl-phosphatidylinositol (GPI)- attachment signal. Seven additional ORFs were found to belong to this group. Upon examination of the possible GPI-attachment sites, it was found that in yeast the most probable amino acids for GPI-attachment are asparagine and glycine. In yeast, GPI-proteins are found at the cell surface, either attached to the plasma-membrane or as an intrinsic part of the cell wall. It was noted that plasma-membrane GPI-proteins possess a dibasic residue motif just before their predicted GPI-attachment site. Based on this, and on homologies between proteins, families of plasma-membrane and cell wall proteins were assigned, revealing 20 potential plasma-membrane and 38 potential cell wall proteins. For members of three plasma-membrane protein families, a function has been described. On the other hand, most of the cell wall proteins seem to be structural components of the wall, responsive to different growth conditions. The GPI-attachment site of yeast slightly differs from mammalian cells. This might be of use in the development of anti-fungal drugs. GPI-ANCHOR GPI-ATTACHMENT SITE YEAST ASCOMYCETES FUNGI https://drive.google.com/file/d/1bN_kIqGQD5IKExYa7C1iSOxMAvg7W4UN/view?usp=drivesdk https://drive.google.com/file/d/1bN_kIqGQD5IKExYa7C1iSOxMAvg7W4UN/view?usp=drivesdk 250602 20260521091201.0