Schmidt Martin, Strenk Meghan E, Boyer Michael P, Fritsch Bryan J
Department of Biochemistry and Nutrition, Des Moines University, 3200 Grand Avenue, Des Moines, IA 50312, USA.
Yeast. 2005 Jul 15;22(9):715-23. doi: 10.1002/yea.1242.
The mannosyltransferase mutants mnn9 and mnn10 were isolated in a genetic screen for septation defects in Saccharomyces cerevisiae. Ultrastructural examination of mutant cell walls revealed markedly thin septal structures and occasional failure to construct trilaminar septa, which then led to the formation of bulky default septa at the bud neck. In the absence of a functional septation apparatus, mnn10 mutants are unable to complete cytokinesis and die as cell chains with incompletely separated cytoplasms, indicating that mannosylation defects impair the ability to form remedial septa. We could not detect N-linked glycosylation of the beta(1,3)glucan synthase Fks1p and mnn10 defects do not change the molecular weight or abundance of the protein. We discuss a model explaining the pleiotropic effects of impaired N-linked protein glycosylation on septation in S. cerevisiae.
甘露糖基转移酶突变体mnn9和mnn10是在酿酒酵母隔膜缺陷的遗传筛选中分离得到的。对突变细胞壁的超微结构检查显示,隔膜结构明显变薄,偶尔无法构建三层隔膜,进而导致在芽颈处形成粗大的默认隔膜。在缺乏功能性隔膜装置的情况下,mnn10突变体无法完成胞质分裂,并以细胞质未完全分离的细胞链形式死亡,这表明甘露糖基化缺陷损害了形成补救隔膜的能力。我们无法检测到β(1,3)葡聚糖合酶Fks1p的N-连接糖基化,且mnn10缺陷不会改变该蛋白的分子量或丰度。我们讨论了一个模型,该模型解释了N-连接蛋白糖基化受损对酿酒酵母隔膜形成的多效性影响。