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首页> 外文期刊>Biochemistry >Vma9p Need Not Be Associated with the Yeast V-ATPase for Fully-Coupled Proton Pumping Activity in Vitro
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Vma9p Need Not Be Associated with the Yeast V-ATPase for Fully-Coupled Proton Pumping Activity in Vitro

机译：Vma9p不需要与酵母V-ATPase相关联的完全耦合的质子体外泵浦活性

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摘要

Vacuolar-type ATPases (V-ATPases) acidify numerous intracellular compartments in all eukaryotic cells and are responsible for extracellular acidification in some specialized cells. V-ATPases are large macromolecular complexes with at least 15 different subunits, some of which are found in multiple copies. The main roles of all V-ATPase subunits have been established except for the e subunit, encoded by the gene VMA9 in Saccharomyces cerevisiae, and the Ac45 subunit, which is not found in the S. cerevisiae enzyme. Here we demonstrate that when the S. cerevisiae V-ATPase is solubilized with the detergent dodecylmaltoside (DDM), Vma9p is removed. We further demonstrate that after Vma9p has been removed by detergent the purified enzyme is still able to perform fully-coupled ATP-dependent proton pumping. This observation shows that Vma9p is not necessary in vitro for this principal activity of the V-ATPase.
机译：液泡型ATP酶（V-ATPase）酸化所有真核细胞中的许多细胞内区室，并负责某些专门细胞中的细胞外酸化。 V-ATPase是具有至少15个不同亚基的大分子复合物，其中一些存在多个副本。已经确定了所有V-ATPase亚基的主要作用，除了由酿酒酵母基因VMA9编码的e亚基和在酿酒酵母酶中未发现的Ac45亚基。在这里，我们证明了当酿酒酵母V-ATPase与去污剂十二烷基麦芽糖苷（DDM）溶解时，Vma9p被去除。我们进一步证明，在Vma9p被去污剂去除后，纯化的酶仍然能够进行完全耦合的ATP依赖质子泵浦。该观察结果表明，Vma9p对于V-ATPase的这一主要活性在体外不是必需的。

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