In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins ofSaccharomyces cerevisiae
✍ Scribed by Caro, L. Heleen P.; Tettelin, Hervé; Vossen, Jack H.; Ram, Arthur F. J.; Van Den Ende, Herman; Klis, Frans M.
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 102 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0749-503X
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✦ Synopsis
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.