Abstract The aspartate:alanine exchanger family of membrane transporters includes industrially important transporters such as succinate exporter and glutamate exporter. No high-resolution structure is available from this family so far, and the transport mechanism of these transporters also remains unclear. In the present study, we focus on the oligomeric status of the aspartate:alanine antiporter (AspT) of Tetragenococcus halophilus, which is the prototype of this family. To investigate the oligomeric structure of AspT, we established a system that produces high yields of highly purified AspT and determined the oligomeric structure of AspT by analysis with size exclusion chromatography coupled with multi-angle light scattering and blue native PAGE and by comparison of the wild-type AspT with a single-cysteine mutant that forms spontaneous inter-molecular thiol crosslinking. All the results consistently support the notion that AspT is a homodimer in solutions and in membranes.
Oligomeric state of the aspartate:alanine transporter from Tetragenococcus halophilus
Akari Miyamoto,T. Yamanaka,Satomi Suzuki,Kota Kunii,Kenichiro Kurono,A. Yoshimi,Masafumi Hidaka,Satoshi Ogasawara,Kei Nanatani,Keietsu Abe
Published 2022 in Journal of Biochemistry (Tokyo)
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- Publication year
2022
- Venue
Journal of Biochemistry (Tokyo)
- Publication date
2022-07-11
- Fields of study
Biology, Medicine, Chemistry
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Semantic Scholar, PubMed
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