Open AccessVanadate-resistant yeast mutants are defective in protein glycosylation.
Author(s) -
Lun Ballou,
Ronald A. Hitzeman,
M. Lewis,
Clinton E. Ballou
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.8.3209
Subject(s) - mutant , glycosylation , complementation , hygromycin b , vanadate , saccharomyces cerevisiae , phenotype , glycoprotein , yeast , biology , genetics , gene , biochemistry
Spontaneous recessive orthovanadate-resistant mutants of Saccharomyces cerevisiae were obtained in five complementation groups, and all show defects in protein glycosylation that mimic the previously isolated mnn mutants. Three of the groups are allelic to the known mnn8, mnn9, and mnn10 mutants, whereas the other two groups show other glycosylation defects. The vanadate-resistant phenotype was associated with enhanced hygromycin B sensitivity. The glycosylation phenotypes of the mutants are all reflections of defects in glycoprotein trafficking, and the easy isolation of vanadate-resistant or hygromycin B-sensitive mutants should facilitate the study of this process.