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首页> 外文期刊>Molecular biology of the cell >The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae
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The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae

机译：在酿酒酵母中，重建的祖先亚基a既充当V-ATPase亚型Vph1p，又充当Stv1p

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摘要

The vacuolar-type, proton-translocating ATPase (V-ATPase) is a multisubunit enzyme responsible for organelle acidification in eukaryotic cells. Many organisms have evolved V-ATPase subunit isoforms that allow for increased specialization of this critical enzyme. Differential targeting of the V-ATPase to specific subcellular organelles occurs in eukaryotes from humans to budding yeast. In Saccharomyces cerevisiae , the two subunit a isoforms are the only difference between the two V-ATPase populations. Incorporation of Vph1p or Stv1p into the V-ATPase dictates the localization of the V-ATPase to the vacuole or late Golgi/endosome, respectively. A duplication event within fungi gave rise to two subunit a genes. We used ancestral gene reconstruction to generate the most recent common ancestor of Vph1p and Stv1p (Anc.a) and tested its function in yeast. Anc.a localized to both the Golgi/endosomal network and vacuolar membrane and acidified these compartments as part of a hybrid V-ATPase complex. Trafficking of Anc.a did not require retrograde transport from the late endosome to the Golgi that has evolved for retrieval of the Stv1p isoform. Rather, Anc.a localized to both structures through slowed anterograde transport en route to the vacuole. Our results suggest an evolutionary model that describes the differential localization of the two yeast V-ATPase isoforms.
机译：液泡型质子转运ATP酶（V-ATPase）是负责真核细胞中细胞器酸化的多亚基酶。许多生物已经进化出V-ATPase亚基同种型，可以增加这种关键酶的特异性。 V-ATPase对特定亚细胞器的差异靶向发生在从人到发芽酵母的真核生物中。在酿酒酵母中，两个亚基a亚型是两个V-ATPase群体之间的唯一区别。 Vph1p或Stv1p掺入V-ATPase决定了V-ATPase分别位于液泡或晚期高尔基体/内体。真菌内的复制事件产生了两个亚基a基因。我们使用祖先的基因重建来生成Vph1p和Stv1p（Anc.a）的最新共同祖先，并测试了其在酵母中的功能。 Anc.a定位于高尔基体/内体网络和液泡膜，并酸化了这些部分，作为杂合V-ATPase复合物的一部分。 Anc.a的贩运不需要从晚期的内体向向高斯基的逆行转运，而高尔基体已进化为可检索Stv1p亚型。相反，Anc.a通过缓慢的顺行转运在到达液泡的过程中定位于两个结构。我们的结果提出了一个进化模型，该模型描述了两种酵母V-ATPase同工型的差异化定位。

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