title: Characterization of CAX4, an Arabidopsis H(+)/cation antiporter.
abstract: Ion compartmentalization is essential for plant growth and development. The Arabidopsis open reading frames for CAX1, CAX2, and CAX3 (cation exchangers 1, 2, and 3) were previously identified as transporters that may modulate ion fluxes across the vacuolar membrane. To understand the diversity and role of H(+)/cation transporters in controlling plant ion levels, another homolog of the CAX genes, CAX4, was cloned from an Arabidopsis cDNA library. CAX4 is 53% identical to CAX1 at the amino acid level, 42% identical to CAX2, and 54% identical to CAX3. CAX4 transcripts appeared to be expressed at low levels in all tissues and levels of CAX4 RNA increased after Mn(2+), Na(+), and Ni(2+) treatment. An N-terminal CAX4-hemagglutinin fusion appeared to localize to both yeast and plant vacuolar membranes. When expressed in yeast, CAX4, like CAX3, failed to suppress the Ca(2+) sensitivity of yeast strains deficient in vacuolar Ca(2+) transport. Several modifications to CAX4 allowed the protein to transport Ca(2+). Addition of amino acids to the N terminus of CAX4 and CAX3 caused both transporters to suppress the sensitivity of yeast strains deficient in vacuolar Ca(2+) transport. These findings suggest that CAX transporters may modulate their ion transport properties through alterations at the N terminus.
authors.affiliation: Baylor College of Medicine, Plant Physiology Group, United States Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, 1100 Bates Street, Houston, TX 77030, USA.
authors.forename: Ning-hui
authors.initials: NH
authors.lastname: Cheng
authors.forename: Jon K
authors.initials: JK
authors.lastname: Pittman
authors.forename: Toshiro
authors.initials: T
authors.lastname: Shigaki
authors.forename: Kendal D
authors.initials: KD
authors.lastname: Hirschi
mesh_terms: D000595:Amino Acid Sequence; D017920:Antiporters / Q000235:genetics* / Q000378:metabolism; D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D027682:Cation Transport Proteins; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D006859:Hydrogen / Q000378:metabolism; D008345:Manganese / Q000494:pharmacology; D008969:Molecular Sequence Data; D009532:Nickel / Q000494:pharmacology; D030821:Plants, Genetically Modified; D012441:Saccharomyces cerevisiae / Q000235:genetics; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D012964:Sodium / Q000494:pharmacology; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism
chemical_list: D017920:Antiporters; D029681:Arabidopsis Proteins; C460090:CAX4 protein, Arabidopsis; D002135:Calcium-Binding Proteins; D027682:Cation Transport Proteins; D018076:DNA, Complementary; C027614:calcium-hydrogen antiporters; D008345:Manganese; D009532:Nickel; D006859:Hydrogen; D012964:Sodium; D002118:Calcium