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Mobility of Stv1p and Vph1p, the 'a' subunit isoforms of the Saccharomyces cerevisiae vacuolar ATPase through late secretory pathway membranes

机译:STV1P和VPH1P的流动性,通过晚期分泌途径膜的酿酒酵母酿酒厂的“A”亚基同种型

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In this work, we have checked several Golgi functions related to N-glycosylation in order to determine how Vph1p, the vacuole located isoform of the V-ATPase, can compensate the lack of the Golgi located Stv1p, in STV1 deleted strains. The lack of the common subunits Vma2p or Vma3p resulted in a defective Golgi function, leading to a significant reduction of the mannosylphospahte transfer and a slight reduction in the outer chain elongation and terminal mannoses addition. As expected, when Vph1p was not present, no effect on glycosylation was detected. Unexpectedly, when the Golgi-specific subunit of the V-ATPase, Stv1p, was absent, N-glycosylation was not affcted. This finding suggests that the vacuolar subunit Vph1p may compensate the lack of the Golgi Stv1p. To confirm this hypothesis, a double mutant lacking both subunits was constructed. In the double mutant, N-glycosylation processes were affected to the same extent as in vma mutants. These results reveal that the Golgi-specific Stv1p can be substituted by the vacuole-specific Vph1p, in stv1delta strains and suggests that the location determinants of the "a" subunit isoforms are not very strict, allowing them to travel to different locations, when needed.
机译:在这项工作中,我们已经检查了与N-糖基化相关的几种Golgi功能,以确定Vph1p如何vph1p,V-ATP酶的同种型,可以补偿STV1缺失的菌株中的缺乏Golgi位于STV1P。缺乏常见的亚基VMA2P或VMA3P导致GOLGI缺陷函数,导致甘露糖基干的显着降低,外链伸长率和终端略微减少。如预期的那样,当没有存在Vph1p时,检测到对糖基化的影响。出乎意料的是,当不存在V-ATP酶的GOLGI特异性亚基时,不粘附N-糖基化。该发现表明,真空亚单​​位Vph1p可以补偿缺乏GOLGI STV1P。为了确认这一假设,构建了缺乏两个亚基的双突变体。在双突变体中,N-糖基化方法在与VMA突变体中的程度相同。这些结果表明,GOLGI特异性STV1P可以在STV1Delta菌株中被液泡特异性Vph1p取代,并表明“A”亚基同种型的位置决定因素不是非常严格,允许它们在需要时向不同的位置行进。

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