Potassium transport at the plasma membrane of the food spoilage yeastZygosaccharomyces bailii

Yeast ◽  
2005 ◽  
Vol 22 (1) ◽  
pp. 21-29 ◽  
Author(s):  
Vadim Demidchik ◽  
Neil Macpherson ◽  
Julia M. Davies
Keyword(s):  
Plasma Membrane ◽  
Potassium Transport ◽  
Food Spoilage

Plasma membrane H+ and K+ transporters are involved in the weak-acid preservative response of disparate food spoilage yeasts

Microbiology ◽  
2005 ◽  
Vol 151 (6) ◽  
pp. 1995-2003 ◽  
Author(s):  
Neil Macpherson ◽  
Lana Shabala ◽  
Henrietta Rooney ◽  
Marcus G. Jarman ◽  
Julia M. Davies
Keyword(s):  
Plasma Membrane ◽  
Benzoic Acid ◽  
Acid Stress ◽  
Weak Acid ◽  
Uptake System ◽  
Food Spoilage ◽  
Adaptive Responses ◽  
Spoilage Yeasts ◽  
Food Spoilage Yeasts

The food spoilage yeasts Zygosaccharomyces bailii and Saccharomyces cerevisiae have been proposed to resist weak-acid preservative stress by different means; Z. bailii by limiting influx of preservative combined with its catabolism, S. cerevisiae by active extrusion of the preservative weak-acid anion and H+. Measurement of H+ extrusion by exponential-phase Z. bailii cells suggest that, in common with S. cerevisiae, this yeast uses a plasma membrane H+-ATPase to expel H+ when challenged by weak-acid preservative (benzoic acid). Simultaneous measurement of Z. bailii net H+ and K+ fluxes showed that net K+ influx accompanies net H+ efflux during acute benzoic acid stress. Such ionic coupling is known for S. cerevisiae in short-term preservative stress. Both yeasts significantly accumulated K+ on long-term exposure to benzoic acid. Analysis of S. cerevisiae K+ transporter mutants revealed that loss of the high affinity K+ uptake system Trk1 confers sensitivity to growth in preservative. The results suggest that cation accumulation is an important factor in adaptation to weak-acid preservatives by spoilage yeasts and that Z. bailii and S. cerevisiae share hitherto unsuspected adaptive responses at the level of plasma membrane ion transport.

scholarly journals ACTIVE TRANSPORT BY THE CECROPIA MIDGUT

1966 ◽  
Vol 31 (1) ◽  
pp. 107-134 ◽  
Author(s):  
Everett Anderson ◽  
William R. Harvey
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Goblet Cell ◽  
Plasma Membranes ◽  
Goblet Cells ◽  
Potassium Transport ◽  
Columnar Cell ◽  
Morphological Data ◽  
Basal Region ◽  
Cytoplasmic Matrix

A morphological basis for transcellular potassium transport in the midgut of the mature fifth instar larvae of Hyalophora cecropia has been established through studies with the light and electron microscopes. The single-layered epithelium consists of two distinct cell types, the columnar cell and the goblet cell. No regenerative cells are present. Both columnar and goblet cells rest on a well developed basement lamina. The basal portion of the columnar cell is incompletely divided into compartments by deep infoldings of the plasma membrane, whereas the apical end consists of numerous cytoplasmic projections, each of which is covered with a fine fuzzy or filamentous material. The cytoplasm of this cell contains large amounts of rough endoplasmic reticulum, microtubules, and mitochondria. In the basal region of the cell the mitochondria are oriented parallel to the long axes of the folded plasma-lemma, but in the intermediate and apical portions they are randomly scattered within the cytoplasmic matrix. Compared to the columnar cell, the goblet cell has relatively little endoplasmic reticulum. On the other hand, the plications of the plasma membrane of the goblet cell greatly exceed those of the columnar cell. One can distinguish at least four characteristic types of folding: (a) basal podocytelike extensions, (b) lateral evaginations, (c) apical microvilli, and (d) specialized cytoplasmic projections which line the goblet chamber. Apically, the projections are large and branch to form villus-like units, whereas in the major portion of the cavity each projection appears to contain an elongate mitochondrion. Junctional complexes of similar kind and position appear between neighboring columnar cells and between adjacent columnar and goblet cells as follows: a zonula adherens is found near the luminal surface and is followed by one or more zonulae occludentes. The morphological data obtained in this study and the physiological information on ion transport through the midgut epithelium have encouraged us to suggest that the goblet cell may be the principal unit of active potassium transport from the hemolymph to the lumen of the midgut. We have postulated that ion accumulation by mitochondria in close association with plicated plasma membranes may play a role in the active movement of potassium across the midgut.

Plasma membrane NADH dehydrogenase and Ca2+-dependent potassium transport in erythrocytes of several animal species

1983 ◽  
Vol 727 (2) ◽  
pp. 266-272 ◽  
Author(s):  
Cristina Miner ◽  
Silvia López-Burillo ◽  
Javier García-Sancho ◽  
Benito Herreros
Keyword(s):  
Plasma Membrane ◽  
Nadh Dehydrogenase ◽  
Animal Species ◽  
Potassium Transport

scholarly journals TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae.

1988 ◽  
Vol 8 (7) ◽  
pp. 2848-2859 ◽  
Author(s):  
R F Gaber ◽  
C A Styles ◽  
G R Fink
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Functional Independence ◽  
Potassium Transport ◽  
Transport Systems ◽  
Plasma Membrane Protein ◽  
Plasma Membrane Atpase ◽  
High Affinity ◽  
Membrane Spanning

We identified a 180-kilodalton plasma membrane protein in Saccharomyces cerevisiae required for high-affinity transport (uptake) of potassium. The gene that encodes this putative potassium transporter (TRK1) was cloned by its ability to relieve the potassium transport defect in trk1 cells. TRK1 encodes a protein 1,235 amino acids long that contains 12 potential membrane-spanning domains. Our results demonstrate the physical and functional independence of the yeast potassium and proton transport systems. TRK1 is nonessential in S. cerevisiae and maps to a locus unlinked to PMA1, the gene that encodes the plasma membrane ATPase. Haploid cells that contain a null allele of TRK1 (trk1 delta) rely on a low-affinity transporter for potassium uptake and, under certain conditions, exhibit energy-dependent loss of potassium, directly exposing the activity of a transporter responsible for the efflux of this ion.

TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae

1988 ◽  
Vol 8 (7) ◽  
pp. 2848-2859 ◽  
Author(s):  
R F Gaber ◽  
C A Styles ◽  
G R Fink
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Functional Independence ◽  
Potassium Transport ◽  
Transport Systems ◽  
Plasma Membrane Protein ◽  
Plasma Membrane Atpase ◽  
High Affinity ◽  
Membrane Spanning

We identified a 180-kilodalton plasma membrane protein in Saccharomyces cerevisiae required for high-affinity transport (uptake) of potassium. The gene that encodes this putative potassium transporter (TRK1) was cloned by its ability to relieve the potassium transport defect in trk1 cells. TRK1 encodes a protein 1,235 amino acids long that contains 12 potential membrane-spanning domains. Our results demonstrate the physical and functional independence of the yeast potassium and proton transport systems. TRK1 is nonessential in S. cerevisiae and maps to a locus unlinked to PMA1, the gene that encodes the plasma membrane ATPase. Haploid cells that contain a null allele of TRK1 (trk1 delta) rely on a low-affinity transporter for potassium uptake and, under certain conditions, exhibit energy-dependent loss of potassium, directly exposing the activity of a transporter responsible for the efflux of this ion.

Heterogeneity of Size and Distribution of Intramembrane Particles in the Plasma Membrane of Yeast

1977 ◽  
Vol 35 ◽  
pp. 596-597
Author(s):  
E. Keyhani
Keyword(s):  
Plasma Membrane ◽  
Candida Utilis ◽  
Synthetic Medium ◽  
Freeze Fracture ◽  
Translational Diffusion ◽  
Yeast Cells ◽  
Distilled Water ◽  
Intramembrane Particles ◽  
The Matrix ◽  
Water Cell

The matrix of biological membranes consists of a lipid bilayer into which proteins or protein aggregates are intercalated. Freeze-fracture techni- ques permit these proteins, perhaps in association with lipids, to be visualized in the hydrophobic regions of the membrane. Thus, numerous intramembrane particles (IMP) have been found on the fracture faces of membranes from a wide variety of cells (1-3). A recognized property of IMP is their tendency to form aggregates in response to changes in experi- mental conditions (4,5), perhaps as a result of translational diffusion through the viscous plane of the membrane. The purpose of this communica- tion is to describe the distribution and size of IMP in the plasma membrane of yeast (Candida utilis).Yeast cells (ATCC 8205) were grown in synthetic medium (6), and then harvested after 16 hours of culture, and washed twice in distilled water. Cell pellets were suspended in growth medium supplemented with 30% glycerol and incubated for 30 minutes at 0°C, centrifuged, and prepared for freeze-fracture, as described earlier (2,3).

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