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Titolo:
THE SPTRK GENE ENCODES A POTASSIUM-SPECIFIC TRANSPORT PROTEIN TKHP INSCHIZOSACCHAROMYCES-POMBE
Autore:
LICHTENBERGFRATE H; REID JD; HEYER M; HOFER M;
Indirizzi:
UNIV BONN,INST BOT D-53115 BONN GERMANY GLAXO INST MOLEC BIOL SA CH-1228 GENEVA SWITZERLAND
Titolo Testata:
The Journal of membrane biology
fascicolo: 2, volume: 152, anno: 1996,
pagine: 169 - 181
SICI:
0022-2631(1996)152:2<169:TSGEAP>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA-MEMBRANE ATPASE; SACCHAROMYCES-CEREVISIAE; FUNCTIONAL EXPRESSION; K+ TRANSPORTERS; SEQUENCE; YEAST; CHANNEL; CDNA; TRK2; DISRUPTION;
Keywords:
K+ UPTAKE SYSTEM; GENETIC COMPLEMENTATION; TRANSPORT KINETICS; PATCH-CLAMP ANALYSIS; ION-SELECTIVITY; SCHIZOSACCHAROMYCES POMBE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
H. Lichtenbergfrate et al., "THE SPTRK GENE ENCODES A POTASSIUM-SPECIFIC TRANSPORT PROTEIN TKHP INSCHIZOSACCHAROMYCES-POMBE", The Journal of membrane biology, 152(2), 1996, pp. 169-181

Abstract

Complementary DNAs involved in potassium transport in Schizosaccharomyces pombe were selected by complementation of defective K+ uptake in a trk1 trk2 mutant of Saccharomyces cerevisiae. Here we describe the SpTRK gene that encodes a protein of 833 amino acids. The predicted structure contains 12 putative membrane-spanning domains and resembles various high- and low-affinity systems for K+ transport in yeasts and plants. TKHp, the product of SpTRK exhibits high homology to TRK1 and TRK2 of Saccharomyces cerevisiae as well as to HKT1 of Triticum aestivum, but is not related to HAK1 of another ascomycete, Schwanniomyces occidentalis, suggesting that different routes for potassium uptake evolved independently. This protein is a potassium-specific transporter since functional analysis of the SpTRK complemented mutant strain of Sacch. cerevisiae revealed potassium transport affinities and uptake characteristics similar to those obtained in wild-type Sch. pombe. Patch-clamp analysis in the whole-cell mode confirmed the TKHp-mediated inwardcurrent in the complemented strain. The inward current increased by acidification of the extracellular medium thereby suggesting a mechanism of K+H+ cotransport. The inward current is not detectable when external K+ is substituted by Na+, documenting a distinct cation specificity of the protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 15:27:57