Anderson J A, Best L A, Gaber R F
Department of Biochemistry, Molecular and Cell Biology, Northwestern University, Evanston, IL 60208.
Gene. 1991 Mar 1;99(1):39-46. doi: 10.1016/0378-1119(91)90031-6.
In Saccharomyces cerevisiae, high-affinity K+ uptake is dependent upon a 180-kDa plasma membrane protein encoded by TRK1 (c-TRK1) [Gaber et al., Mol. Cell. Biol. 8 (1988) 2848-2859)]. Although hybridization with a c-TRK1 probe revealed highly homologous sequences in the genomes of most Saccharomyces species, the TRK1 sequence in S. uvarum (u-TRK1) was detected only under low-stringency conditions. We cloned u-TRK1 and found it to confer high-affinity K+ uptake in S. cerevisiae. A comparison of the inferred amino acid sequences reveals 78% identity and 86% similarity between the two high-affinity transporters. The most highly conserved regions are the putative membrane-spanning domains (95% identical), suggesting that the structure of the transmembrane domains is important for high-affinity K+ transport.
在酿酒酵母中,高亲和力钾离子摄取依赖于由TRK1(c-TRK1)编码的一种180 kDa的质膜蛋白[加伯等人,《分子与细胞生物学》8(1988)2848 - 2859]。尽管与c-TRK1探针杂交显示在大多数酿酒酵母物种的基因组中存在高度同源序列,但仅在低严格条件下才检测到葡萄汁酵母(u-TRK1)中的TRK1序列。我们克隆了u-TRK1,并发现它能赋予酿酒酵母高亲和力钾离子摄取能力。对推导的氨基酸序列进行比较发现,这两种高亲和力转运蛋白之间有78%的同一性和86%的相似性。最保守的区域是假定的跨膜结构域(95%相同),这表明跨膜结构域的结构对于高亲和力钾离子转运很重要。