VANADATE-RESISTANT YEAST MUTANTS ARE DEFECTIVE IN PROTEIN GLYCOSYLATION

被引：124

作者：

BALLOU, L ^{[1
]}

HITZEMAN, RA ^{[1
]}

LEWIS, MS ^{[1
]}

BALLOU, CE ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY, DEPT MOLEC & CELL BIOL, DIV BIOCHEM & MOLEC BIOL, BERKELEY, CA 94720 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 08期

关键词：

D O I：

10.1073/pnas.88.8.3209

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

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.

引用

页码：3209 / 3212

页数：4

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