PRIMARY STRUCTURE OF THE URACIL TRANSPORT PROTEIN OF SACCHAROMYCES-CEREVISIAE
PRIMARY STRUCTURE OF THE URACIL TRANSPORT PROTEIN OF SACCHAROMYCES-CEREVISIAE
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DOI：
10.1111/j.1432-1033.1988.tb13806.x
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发表时间：
1988-01-15
期刊：
影响因子：
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通讯作者：
CHEVALLIER, MR
中科院分区：
文献类型：
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作者：
JUND, R;WEBER, E;CHEVALLIER, MR
本文报道了酿酒酵母中编码尿嘧啶渗透酶的FUR4基因的核苷酸序列。推导的氨基酸序列为633个残基，由许多疏水伸展组成，只有蛋白质的N末端(分别约100和50个氨基酸)是主要亲水性的。虽然这项工作表明尿嘧啶通透酶的生物合成通过分泌/糖基化途径，但不存在N端疏水信号肽。使用三种不同方法的结果，允许预测跨膜α。在蛋白质序列中，我们绘制了膜中渗透酶折叠的模型。
We present in this paper the nucleotidic sequence of the FUR4 gene encoding the uracil permease in the yeast Saccharomyces cerevisiae. The deduced amino acid sequence of the permease has 633 residues; it consists of many hydrophobic stretches, only the N-terminal ends of the protein (about 100 and 50 amino acids respectively) being mostly hydrophilic. No N-terminal hydrophobic signal peptide is present, although it is shown in this work that the biosynthesis of the uracil permease goes through the secretion/glycosylation pathway. Using the results of three different methods, allowing the prediction of transmembrane .alpha. helices in proteic sequences, we draw a model of folding of the permease in the membrane.