|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:dateCreated |
1999-1-13
|
|
pubmed:abstractText |
The NHA1 gene of Saccharomyces cerevisiae, transcribed into a 3.5 kb mRNA, encodes a protein mediating Na+ and K+ efflux through the plasma membrane that is required for alkali cation tolerance at acidic pH. Deletion of the gene in a wild-type strain resulted in higher sensitivity to both K+ and Na+ at acidic pH. Measurements of cation loss in strains carrying deleted or overexpressed alleles of NHA1 demonstrated its role in K+ and Na+ efflux. In addition, high K+ and Na+ efflux observed upon alkalinization of the cytoplasm implies a role of Nha1p in the regulation of intracellular pH. Moreover, the overexpression of ENA1 and NHA1 genes in an ena1-4 delta-nha1 delta strain showed that the Nha1 alkalication antiporter is responsible for growth on high concentrations of KCl and NaCl at acidic pH, and Ena alkali-cation ATPases are necessary at higher pH values. Both systems have a complementary action to maintain the intracellular steady-state concentration of K+ and Na+.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ENA1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NHA1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium-Hydrogen Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
1350-0872
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
144 ( Pt 10)
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2749-58
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9802016-Adenosine Triphosphatases,
pubmed-meshheading:9802016-Antiporters,
pubmed-meshheading:9802016-Blotting, Northern,
pubmed-meshheading:9802016-Blotting, Western,
pubmed-meshheading:9802016-Cation Transport Proteins,
pubmed-meshheading:9802016-Cloning, Molecular,
pubmed-meshheading:9802016-Drug Tolerance,
pubmed-meshheading:9802016-Fungal Proteins,
pubmed-meshheading:9802016-Gene Deletion,
pubmed-meshheading:9802016-Gene Expression,
pubmed-meshheading:9802016-Genetic Vectors,
pubmed-meshheading:9802016-Homeostasis,
pubmed-meshheading:9802016-Hydrogen-Ion Concentration,
pubmed-meshheading:9802016-Ion Transport,
pubmed-meshheading:9802016-Membrane Proteins,
pubmed-meshheading:9802016-Potassium,
pubmed-meshheading:9802016-Potassium-Hydrogen Antiporters,
pubmed-meshheading:9802016-Promoter Regions, Genetic,
pubmed-meshheading:9802016-Saccharomyces cerevisiae,
pubmed-meshheading:9802016-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9802016-Salts,
pubmed-meshheading:9802016-Sodium,
pubmed-meshheading:9802016-Sodium-Hydrogen Antiporter,
pubmed-meshheading:9802016-Sodium-Potassium-Exchanging ATPase
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
The Nha1 antiporter of Saccharomyces cerevisiae mediates sodium and potassium efflux.
|
|
pubmed:affiliation |
Laboratoire de Microbiologie et de Génétique, Université Louis Pasteur/CNRS, Strasbourg, France.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
