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AtHMA3, a plant P 1B ‐ATPase, functions as a Cd/Pb transporter in yeast
Author(s) -
Gravot Antoine,
Lieutaud Aurélie,
Verret Frédéric,
Auroy Pascaline,
Vavasseur Alain,
Richaud Pierre
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00072-9
Subject(s) - vacuole , arabidopsis thaliana , atpase , cadmium , mutant , biochemistry , green fluorescent protein , transporter , yeast , atp binding cassette transporter , biology , transport protein , microbiology and biotechnology , chemistry , enzyme , gene , cytoplasm , organic chemistry
The Arabidopsis thaliana AtHMA3 protein belongs to the P 1B ‐adenosine triphosphatase (ATPase) transporter family, involved in heavy metal transport. Functional expression of AtHMA3 phenotypically complements the Cd/Pb‐hypersensitive yeast strain Δ ycf1 , but not the Zn‐hypersensitive mutant Δ zrc1 . AtHMA3‐complemented Δ ycf1 cells accumulate the same amount of cadmium as YCF1‐complemented Δ ycf1 cells or wild‐type cells, suggesting that AtHMA3 carries out an intracellular sequestration of Cd. A mutant of AtHMA3 altered in the P‐ATPase phosphorylation domain did not complement Δ ycf1 , suggesting that metal transport rather than chelation is involved. The fusion protein AtHMA3::green fluorescent protein (GFP) is localized at the vacuole, consistent with a role in the influx of cadmium into the vacuolar compartment. In A. thaliana , the mRNA of AtHMA3 was detected mainly in roots, old rosette leaves and cauline leaves. The expression levels were not affected by cadmium or zinc treatments.