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  • 标题:Vanadate-resistant yeast mutants are defective in protein glycosylation.
  • 本地全文:下载
  • 作者:L Ballou ; R A Hitzeman ; M S Lewis
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1991
  • 卷号:88
  • 期号:8
  • 页码:3209-3212
  • DOI:10.1073/pnas.88.8.3209
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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.
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