Dedicated transporters for peptide export and intercompartmental traffic in the yeast Saccharomyces cerevisiae.
Dedicated transporters for peptide export and intercompartmental traffic in the yeast Saccharomyces cerevisiae.
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用于酿酒酵母中肽输出和区室间运输的专用转运蛋白。
DOI：
10.1101/sqb.1992.057.01.064
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Thorner,J
中科院分区：
文献类型：
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作者：
Kuchler,K;Göransson,HM;Viswanathan,MN;Thorner,J
在原核和真核细胞中，都有一些蛋白质驻留在质膜上，催化特定肽、蛋白质和其他大分子的输出。类似的分子位于分隔胞内细胞器的膜上，似乎介导多肽进入这些隔室的进口。负责这些跨膜易位事件的专用转运蛋白都是一个非常大的完整膜蛋白超家族的成员，它们具有广泛的序列相似性和结构域组织，并且还包含一个高度保守的基元，该基元赋予这些转运蛋白结合和水解ATE的能力。这一膜结合转运蛋白家族被称为atp结合盒或“ABC”蛋白（Higgins 1992）或“交通atp酶”（Ames et al. 1990）。这类特化膜蛋白的一个代表成员是酿酒酵母（Saccharomyces cerevisiae）的STE6基因产物（Ste6p） （Kuchler et al. 1989; McGrath and Varshavsky 1989）。在这里，我们回顾了Ste6p是ABC膜结合转运蛋白家族成员的证据，以及Ste6p负责MATa基因型单倍体细胞分泌肽交配信息素（a因子）的研究结果。我们还提供了有关Ste6p的结构、定位和功能的最新数据。以Ste6p为范例，我们还通过实验解决了关于这种转运体的生理作用的其他问题，包括(1)Ste6p是否可以介导酵母细胞中除a因子外的另一种肽的输出；(2) Ste6p的哺乳动物同源物（人类模型基因产物或p -糖蛋白）是否可以在体内替代Ste6p (Endicott and Ling 1989; Gottesman and Pastan 1993)， p -糖蛋白最初因其能够在培养中赋予动物细胞多药耐药性而被发现；(3)一个真核细胞中可能有多少abc型转运蛋白，甚至在像酿酒酵母这样基因组大小相对较小（~ 15 Mb）的生物体中也是如此（Olson 1991）。ura3-52 leu2-3,112 HIS3 - 11,15 trpl1 ade2-1 can - lo0)及其等基因ste6A衍生物WKK7 (ste6A:: HIS3)，构建方法如前所述（Kuchler et al. 1989）。配对试验菌株RC757 (MA Ta sst2-1 rmel his6me1cam cyh2)（Chan and Otte 1982）和
In both prokaryotic and eukaryotic cells, there are proteins that reside in the Plasma membrane which catalyze the export of specific peptides, proteins, and other macromolecules. Similar molecules are located in the membranes that delimit intracellular organelles and appear to mediate the import of polypeptides into these compartments. The dedicated transporters that are responsible for these transmembrane translocation events are all members of a very large superfamily of integral membrane proteins that share extensive sequence similarity and domain organization and also contain a highly conserved motif that confers on these transporters the ability to bind and hydrolyze ATE Hence, this family of membrane-bound transporters has been called the ATP-binding cassette or" ABC" proteins (Higgins 1992) or the" traffic ATPases"(Ames et al. 1990). One representative member of this class of specialized membrane proteins is the STE6 gene product (Ste6p) of the yeast Saccharomyces cerevisiae (Kuchler et al. 1989; McGrath and Varshavsky 1989). Here we review the evidence that Ste6p is a member of the ABC family of membrane-bound transporters and the findings that demonstrate that Ste6p is responsible for the secretion of the peptide mating pheromone, a-factor, from haploid cells of the MATa genotype. We also present more recent data on the structure, localization, and function of Ste6p. Using Ste6p as the paradigm, we also address experimentally additional questions about the physiological role of this type of transporter, including (1) whether Ste6p can mediate the export of another peptide from yeast cells other than a-factor;(2) whether a mammalian homolog of Ste6p, the human mdrl gene product or" P-glycoprotein," first recognized because of its ability to confer multidrug resistance to animal cells in culture (Endicott and Ling 1989; Gottesman and Pastan 1993), can substitute for Ste6p in vivo; and (3) how many ABC-type transporters there might be in a eukaryotic cell, even in an organism, like S. cerevisiae, with a relatively small genome size (~ 15 Mb)(Olson 1991). ura3-52 leu2-3,112 his3-11, 15 trpl-1 ade2-1 canl-lO0) and its isogenic ste6A derivative, WKK7 (ste6A:: HIS3), constructed as described previously (Kuchler et al. 1989). Mating tester strains were RC757 (MA Ta sst2-1 rmel his6 met1 cam cyh2)(Chan and Otte 1982) and