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Research Paper
The Membrane Topology of ALMT1, an Aluminum-Activated Malate Transport Protein in Wheat (Triticum aestivum)
Hirotoshi Motoda, Takayuki Sasaki, Yoshio Kano, Peter R. Ryan, Emmanuel Delhaize, Hideaki Matsumoto and Yoko Yamamoto
volume 2 | issue 6
november/decemberPages: 467 - 472
This is an open-access article
If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.
The wheat ALMT1 gene encodes an aluminum (Al)-activated malate transport protein which confers Al-resistance. We investigated the membrane topology of this plasma-membrane localized protein with immunocytochemical techniques. Several green fluorescent protein (GFP)-fused and histidine (His)-tagged chimeras of ALMT1 were prepared based on a computer-predicted secondary structure and transiently expressed in cultured mammalian cells. Antibodies raised to polypeptide epitopes of ALMT1 were used in conjunction with the antibody to the His-tags to determine the topology of ALMT1. This study shows that the ALMT1 protein contains six transmembrane domains with the amino and carboxyl termini located on the extracellular side of the plasma membrane.
Authors
Hirotoshi Motoda
Research Institute for Bioresources; Okayama University; Okayama, Japan
Takayuki Sasaki
Research Institute for Bioresources; Okayama University; Okayama, Japan
Yoshio Kano
Department of Health Science; Kibi International University; Okayama, Japan
Peter R. Ryan
CSIRO Plant Industry; Canberra, Australia
Emmanuel Delhaize
CSIRO Plant Industry; Canberra, Australia
Hideaki Matsumoto
Okayama University, Kurashiki, Japan
Yoko Yamamoto
Research Institute for Bioresources; Okayama University; Kurashiki, Okayama, Japan
This is an open-access article
If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.




