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首页> 外文期刊>Yeast >Mutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha
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Mutation of the protein-O-mannosyltransferase enhances secretion of the human urokinase-type plasminogen activator in Hansenula polymorpha

机译：蛋白-O-甘露糖基转移酶的突变增强了多形汉逊酵母中人尿激酶型纤溶酶原激活物的分泌

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摘要

Human urokinase-type plasminogen activator (uPA) is poorly secreted and aggregates in the endoplasmic reticulum of yeast cells due to inefficient folding. A screen for Hansenula polymorpha mutants with improved uPA secretion revealed a gene encoding a homologue of the Saccharomyces cerevisiae protein-O-mannosyltransferase Pmt1p. Expression of the H. polymorpha PMT1 gene (HpPMT1) abolished temperature sensitivity of the S. cerevisiae pmt1 pmt2 double mutant. As in S. cerevisiae, inactivation of the HpPMT1 gene affected electrophoretic mobility of the O-glycosylated protein, extracellular chitinase. In contrast to S. cerevisiae, disruption of HpPMT1 alone caused temperature sensitivity. Inactivation of the HpPMT1 gene decreased intracellular aggregation of uPA, suggesting that enhanced secretion of uPA was due to improvement of its folding in the endoplasmic reticulum. Unlike most of the endoplasmic reticulum membrane proteins, HpPmt1p possesses the C-terminal KDEL retention signal.
机译：人尿激酶型纤溶酶原激活剂（uPA）分泌不佳，并且由于折叠效率低而聚集在酵母细胞的内质网中。 uPA分泌改善的多形汉逊酵母突变体的筛选揭示了一个基因，该基因编码啤酒酵母蛋白-O-甘露糖基转移酶Pmt1p的同源物。多形汉逊酵母PMT1基因（HpPMT1）的表达废除了酿酒酵母pmt1 pmt2双突变体的温度敏感性。与酿酒酵母一样，HpPMT1基因的失活会影响O-糖基化蛋白细胞外几丁质酶的电泳迁移率。与酿酒酵母相反，单独破坏HpPMT1会引起温度敏感性。 HpPMT1基因的失活减少了uPA的细胞内聚集，表明uPA的分泌增加是由于其在内质网中折叠的改善所致。与大多数内质网膜蛋白不同，HpPmt1p具有C端KDEL保留信号。

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