Functional identification of AtAVT3, a family of vacuolar amino acid transporters, in Arabidopsis

Amino acids stored in the vacuoles are exported to the cytosol mainly for protein synthesis; however, the molecular identity of vacuolar amino acid exporters remains obscure in plants. Here, we demonstrate that the heterologous expression of AtAVT3 genes, Arabidopsis homologs of AVT3 and AVT4 encodi...

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Bibliographic Details
Published in:FEBS letters 2017-01, Vol.591 (1), p.5-15
Main Authors: Fujiki, Yuki, Teshima, Hiromitsu, Kashiwao, Shinji, Kawano‐Kawada, Miyuki, Ohsumi, Yoshinori, Kakinuma, Yoshimi, Sekito, Takayuki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acid Transport Systems - chemistry
Amino Acid Transport Systems - genetics
Amino Acid Transport Systems - metabolism
amino acid transporter
Amino Acids - metabolism
Arabidopsis
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Biological Transport
export
Gene Expression Regulation, Plant
Intracellular Membranes - metabolism
Phylogeny
Plant Cells - metabolism
Saccharomyces cerevisiae - metabolism
Sequence Homology, Amino Acid
Subcellular Fractions - metabolism
vacuole
Vacuoles - metabolism
yeast
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Summary:Amino acids stored in the vacuoles are exported to the cytosol mainly for protein synthesis; however, the molecular identity of vacuolar amino acid exporters remains obscure in plants. Here, we demonstrate that the heterologous expression of AtAVT3 genes, Arabidopsis homologs of AVT3 and AVT4 encoding vacuolar amino acid exporters in yeast, reduces vacuolar amino acid levels in the avt3∆avt4∆ yeast cells. In vitro experiments revealed that 14C‐labeled Ala and Pro are exported from vacuolar membrane vesicles by AtAvt3A in an ATP‐dependent manner. In Arabidopsis, AtAvt3A fused with green fluorescent protein localizes to the vacuolar membrane. We propose that AtAVT3 family represents the long sought‐for vacuolar amino acid exporters in plants.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12507