Structural and functional conservation between the high-affinity K+ transporters of Saccharomyces uvarum and Saccharomyces cerevisiae
- PMID: 2022322
- DOI: 10.1016/0378-1119(91)90031-6
Structural and functional conservation between the high-affinity K+ transporters of Saccharomyces uvarum and Saccharomyces cerevisiae
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.
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