ArticleMolecular and cellular biochemistry2003
Functional analysis of amino acids of the Na+/H+ exchanger that are important for proton translocation.
Article in Molecular and cellular biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- The Remaining Conundrum of the Role of the NaReviews in cardiovascular medicine · 2022Review
- Structural and functional analysis of transmembrane segment IV of the salt tolerance protein Sod2.The Journal of biological chemistry · 2013Article
- A novel plant vacuolar Na+/H+ antiporter gene evolved by DNA shuffling confers improved salt tolerance in yeast.The Journal of biological chemistry · 2010Article
- Alkali metal cation transport and homeostasis in yeasts.Microbiology and molecular biology reviews : MMBR · 2010Review
- Expression, purification, and reconstitution of the Na(+)/H (+) exchanger sod2 in Saccharomyces cerevisiae.Molecular and cellular biochemistry · 2008Article
- Exploration of yeast alkali metal cation/H+ antiporters: sequence and structure comparison.Folia microbiologica · 2006Article
- New developments in the understanding of the cation diffusion facilitator family.Journal of industrial microbiology & biotechnology · 2005Review
- The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1.Biochemistry · 2005Article
- Identification of conserved polar residues important for salt tolerance by the Na+/H+ exchanger of Schizosaccharomyces pombe.Molecular and cellular biochemistry · 2005Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Na+/H+ exchanger is an integral membrane protein found in the plasma membrane of eukaryotic and prokaryotic cells. In eukaryotes it functions to exchange one proton for a sodium ion. In mammals it removes intracellular protons while in plants and fungal cells the plasma membrane form removes intracellular sodium in exchange for extracellular protons. In this study we used the Na+/H+ exchanger of Schizosaccharomyces pombe (Sod2) as a model system to study amino acids critical for activity of the protein. Twelve mutant forms of the Na+/H+ exchanger were examined for their ability to translocate protons as assessed by a Cytosensor microphysiometer. Mutation of the amino acid Histidine 367 resulted in defective proton translocation. The acidic residues Asp145, Asp178, Asp266 and Asp267 were important in the proton translocation activity of the Na+/H+ exchanger. Mutation of amino acids His98, His233 and Asp241 did not significantly impair proton translocation by the Na+/H+ exchanger. These results confirm that polar amino acids are important in proton flux activity of Na+/H+ exchangers.
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