Characterization of potassium transport in wild-type and isogenic yeast strains carrying all combinations of trk1, trk2 and tok1 null mutations

被引:90
作者
Bertl, A
Ramos, J
Ludwig, J
Lichtenberg-Fraté, H
Reid, J
Bihler, H
Calero, F
Martínez, P
Ljungdah, PO
机构
[1] Ludwig Inst Canc Res, S-10401 Stockholm, Sweden
[2] AstraZeneca, Wilmington, DE USA
[3] Univ Bonn, D-5300 Bonn, Germany
[4] Univ Tubingen, D-72074 Tubingen, Germany
[5] Univ Cordoba, E-14071 Cordoba, Spain
[6] Univ Karlsruhe, Karlsruhe, Germany
关键词
D O I
10.1046/j.1365-2958.2003.03335.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Saccharomyces cerevisiae cells express three defined potassium-specific transport systems encoded by TRK1, TRK2 and TOK1. To gain a more complete understanding of the physiological function of these transport proteins, we have constructed a set of isogenic yeast strains carrying all combinations of trk1Delta, trk2Delta and tok1Delta null mutations. The in vivo K+ transport characteristics of each strain have been documented using growth-based assays, and the in vitro biochemical and electrophysiological properties associated with K+ transport have been determined. As has been reported previously, Trk1p and Trk2p facilitate high-affinity potassium uptake and appear to be functionally redundant under a wide range of environmental conditions. In the absence of TRK1 and TRK2, strains lack the ability specifically to take up K+, and trk1Deltatrk2Delta double mutant cells depend upon poorly understood non-specific cation uptake mechanisms for growth. Under conditions that impair the activity of the non-specific uptake system, termed NSC1, we have found that the presence of functional Tok1p renders cells sensitive to Cs+. Based on this finding, we have established a growth-based assay that monitors the in vivo activity of Tok1p.
引用
收藏
页码:767 / 780
页数:14
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  • [1] A molecular target for viral killer toxin: TOK1 potassium channels
    Ahmed, A
    Sesti, F
    Ilan, N
    Shih, TM
    Sturley, SL
    Goldstein, SAN
    [J]. CELL, 1999, 99 (03) : 283 - 291
  • [2] FUNCTIONAL EXPRESSION OF A PROBABLE ARABIDOPSIS-THALIANA POTASSIUM CHANNEL IN SACCHAROMYCES-CEREVISIAE
    ANDERSON, JA
    HUPRIKAR, SS
    KOCHIAN, LV
    LUCAS, WJ
    GABER, RF
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (09) : 3736 - 3740
  • [3] P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis
    Bañuelos, MA
    Rodríguez-Navarro, A
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (03) : 1640 - 1646
  • [4] Bañuelos MA, 1998, MICROBIOL-UK, V144, P2749, DOI 10.1099/00221287-144-10-2749
  • [5] BERTL A, 1993, J MEMBRANE BIOL, V132, P183
  • [6] USE OF SACCHAROMYCES-CEREVISIAE FOR PATCH-CLAMP ANALYSIS OF HETEROLOGOUS MEMBRANE-PROTEINS - CHARACTERIZATION OF KAT1, AN INWARD-RECTIFYING K+ CHANNEL FROM ARABIDOPSIS-THALIANA, AND COMPARISON WITH ENDOGENEOUS YEAST CHANNELS AND CARRIERS
    BERTL, A
    ANDERSON, JA
    SLAYMAN, CL
    GABER, RF
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (07) : 2701 - 2705
  • [7] Physiological characterization of the yeast plasma membrane outward rectifying K+ channel, DUK1 (TOK1), in situ
    Bertl, A
    Bihler, H
    Reid, JD
    Kettner, C
    Slayman, CL
    [J]. JOURNAL OF MEMBRANE BIOLOGY, 1998, 162 (01) : 67 - 80
  • [8] Electrophysiology in the eukaryotic model cell Saccharomyces cerevisiae
    Bertl, A
    Bihler, H
    Kettner, C
    Slayman, CL
    [J]. PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 1998, 436 (06): : 999 - 1013
  • [9] NSC1:: a novel high-current inward rectifier for cations in the plasma membrane of Saccharomyces cerevisiae
    Bihler, H
    Slayman, CL
    Bertl, A
    [J]. FEBS LETTERS, 1998, 432 (1-2) : 59 - 64
  • [10] Low-affinity potassium uptake by Saccharomyces cerevisiae is mediated by NSCI, a calcium-blocked non-specific cation channel
    Bihler, H
    Slayman, CL
    Bertl, A
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2002, 1558 (02): : 109 - 118