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Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae.

机译:自糖基化引发剂蛋白Glg1p和Glg2p对酿酒酵母中糖原积累的需求。

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摘要

Glycogen, a branched polymer of glucose, is a storage molecule whose accumulation is under rigorous nutritional control in many cells. We report the identification of two Saccharomyces cerevisiae genes, GLG1 and GLG2, whose products are implicated in the biogenesis of glycogen. These genes encode self-glucosylating proteins that in vitro can act as primers for the elongation reaction catalyzed by glycogen synthase. Over a region of 258 residues, the Glg proteins have 55% sequence identify to each other and approximately 33% identity to glycogenin, a mammalian protein postulated to have a role in the initiation of glycogen biosynthesis. Yeast cells defective in either GLG1 or GLG2 are similar to the wild type in their ability to accumulate glycogen. Disruption of both genes results in the inability of the cells to synthesize glycogen despite normal levels of glycogen synthase. These results suggest that a self-glucosylating protein is required for glycogen biosynthesis in a eukaryotic cell. The activation state of glycogen synthase in glg1 glg2 cells is suppressed, suggesting that the Glg proteins may additionally influence the phosphorylation state of glycogen synthase.
机译:糖原是葡萄糖的分支聚合物,是一种存储分子,其积累在许多细胞中都受到严格的营养控制。我们报告鉴定两个酿酒酵母基因,GLG1和GLG2,其产物与糖原的生物发生有关。这些基因编码自糖基化蛋白,其在体外可以充当由糖原合酶催化的延伸反应的引物。在258个残基的区域上,Glg蛋白彼此具有55%的序列同一性,与糖原蛋白(一种假定在糖原生物合成的启动中起作用的哺乳动物蛋白)具有大约33%的同一性。在GLG1或GLG2中有缺陷的酵母细胞在积累糖原方面的能力与野生型相似。尽管糖原合酶水平正常,这两个基因的破坏都会导致细胞无法合成糖原。这些结果表明,真核细胞中糖原生物合成需要自糖基化蛋白。 glg1 glg2细胞中糖原合酶的激活状态被抑制,表明Glg蛋白可能另外影响糖原合酶的磷酸化状态。

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