首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Structural and functional conservation between the high-affinity K+ transporters of Saccharomyces uvarum and Saccharomyces cerevisiae
Authors:J A Anderson  L A Best  R F Gaber
Institution:Department of Biochemistry, Molecular and Cell Biology, Northwestern University, Evanston, IL 60208.
Abstract: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.
Keywords:
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号