The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital

Gentzsch, M and Tanner, W (1996) The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO JOURNAL, 15 (21). pp. 5752-5759. ISSN 0261-4189, 1460-2075

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Abstract

The transfer of mannose to seryl and threonyl residues of secretory proteins is catalyzed by a family of protein mannosyltransferases coded for by seven genes (PMT1-7), Mannose dolichylphosphate is the sugar donor of the reaction, which is localized at the endoplasmic reticulum, By gene disruption and crosses all single, double and triple mutants of genes PMT1-4 were constructed, Two of the double and three of the triple mutants were not able to grow under normal conditions; three of these mutants could grow, however, when osmotically stabilized. The various mutants were extensively characterized concerning growth, morphology and their sensitivity to killer toxin K1, caffeine and calcofluor white, O-Mannosylation of gp115/Gas1p was affected only in pmt4 mutants, whereas glycosylation of chitinase was mainly affected in pmt1 and pmt2 mutants, The results show that protein O-glycosylation is essential for cell wall rigidity and cell integrity and that this protein modification, therefore, is vital for Saccharomyces cerevisiae.

Item Type: Article
Uncontrolled Keywords: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE; D-MANNOSYLTRANSFERASE; CELL-WALL; OSMOTIC STABILITY; D-GALACTOSAMINE; YEAST; SEPARATION; OLIGOSACCHARIDES; PURIFICATION; PHOSPHATASES; glycoprotein; mannosyltransferase; osmotic stability; PMT gene family; yeast
Depositing User: Dr. Gernot Deinzer
Last Modified: 19 Oct 2022 08:34
URI: https://pred.uni-regensburg.de/id/eprint/51371

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