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ATG23, a novel gene required for maturation of proaminopeptidase I, but not for autophagy

机译:ATG23,前氨基肽酶I成熟所需的新基因,但自噬则不需要

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In rich media proaminopeptidase I is targeted to the vacuole via the Cvt pathway and during starvation via autophagy. We here identify Atg23 (Y1r431c), a protein of so far unknown function, as a novel component essential for proaminopeptidase I maturation under non-starvation conditions. Maturation of proaminopeptidase I takes place in starved atg23Delta cells. Selective vacuolar targeting of the autophagosomal marker GFP-Aut7 and the accumulation of autophagic bodies during starvation in the presence of phenyltnethylsulfonyl fluoride suggest that autophagy occurs in atg23Delta cells but at a reduced rate. In atg23Delta cells mature vacuolar carboxypeptidase Y is present and accumulation of quinacrine suggests no significant defect in vacuolar acidification. Furthermore, growth of atg23Delta cells on nitrocellulose detects no significant secretion of carboxypeptidase Y
机译:在丰富的培养基中,前氨基肽酶I通过Cvt途径以及在饥饿期间通过自噬作用靶向液泡。我们在这里确定Atg23(Y1r431c),一种迄今未知功能的蛋白质,是非饥饿条件下原氨肽酶I成熟必不可少的新组分。原氨基肽酶I的成熟发生在饥饿的atg23Delta细胞中。自噬体标记GFP-Aut7的选择性液泡靶向和在饥饿期间在苯基苯乙磺酰氟存在下自噬体的积累表明自噬在atg23Delta细胞中发生,但发生率降低。在atg23Delta细胞中,存在成熟的液泡羧肽酶Y,奎纳克林的积累表明液泡酸化没有明显的缺陷。此外,atg23Delta细胞在硝酸纤维素上的生长未检测到羧肽酶Y的显着分泌

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