SACCHAROMYCES-CEREVISIAE STE6 GENE-PRODUCT - A NOVEL PATHWAY FOR PROTEIN EXPORT IN EUKARYOTIC CELLS
SACCHAROMYCES-CEREVISIAE STE6 GENE-PRODUCT - A NOVEL PATHWAY FOR PROTEIN EXPORT IN EUKARYOTIC CELLS
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DOI：
10.1002/j.1460-2075.1989.tb08580.x
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发表时间：
1989-12-20
期刊：
影响因子：
11.4
通讯作者：
THORNER, J
中科院分区：
文献类型：
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作者：
KUCHLER, K;STERNE, RE;THORNER, J
酿酒酵母Mata细胞释放一种脂肽交配信息素，a-因子。放射性标记和免疫沉淀表明，MATA ste6突变体在细胞内产生前α因子和成熟的α因子，但很少或不产生细胞外信息素。携带同时含有MFa1(前α-因子结构基因)和STE6基因的多拷贝质粒的正常MATA细胞分泌α-因子的速度至少是同一载体中仅携带MFa1的相同细胞的五倍。STE6基因的核苷酸序列预测了一个1290个残基的多肽，具有多个跨膜片段和两个亲水结构域，每个结构域都与一系列特征明确的原核生物渗透层(包括hylB、OPPD、Hisp、Malk和pstB)同源，并与哺乳动物的MDR(多药耐药)转运蛋白有更大的同源性。这些结果表明，酵母中的STE6蛋白，以及动物中的MDR，可能是一种跨膜转运体，通过一条独立于经典分泌途径的途径输出多肽。
Saccharomyces cerevisiae MATa cells release a lipopeptide mating pheromone, a-factor. Radiolabeling and immunoprecipitation show that MATa ste6 mutants produce pro-a-factor and mature a-factor intracellularly, but little or no extracellular pheromone. Normal MATa cells carrying a multicopy plasmid containing both MFa1 (pro-a-factor structural gene) and the STE6 gene secrete a-factor at least five times faster than the same cells carrying only MFa1 in the same vector. The nucleotide sequence of the STE6 gene predicts a 1290 residue polypeptide with multiple membrane spanning segments and two hydrophilic domains, each strikingly homologous to a set of well-characterized prokaryotic permeases (including hylB, oppD, hisP, malK and pstB) and sharing even greater identity with mammalian mdr (multiple drug resistance) transporters. These results suggest that the STE6 protein in yeast, and possibly mdr in animals, is a transmembrane translocater that exports polypeptides by a route independent of the classical secretory pathway.