Abstract
In Saccharomyces cerevisiae, Pho89 mediates a cation-dependent transport of Pi across the plasma membrane. This integral membrane protein belongs to the Inorganic Phosphate Transporter (PiT) family, a group that includes the mammalian Na+/Pi cotransporters Pit1 and Pit2. Here we report that the Pichia pastoris expressed recombinant Pho89 was purified in the presence of Foscholine-12 and functionally reconstituted into proteoliposomes with a similar substrate specificity as observed in an intact cell system. The alpha-helical content of the Pho89 protein was estimated to 44%. EPR analysis showed that purified Pho89 protein undergoes conformational change upon addition of substrate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 551-556 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 436 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 5 2013 |
Keywords
- Circular dichroism
- Oligomer
- Pho89
- Phosphate transport
- Pichia pastoris
- Reconstitution
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
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Cite this
Sengottaiyan, P., Petrlova, J., Lagerstedt, J. O., Ruiz-Pavon, L., Budamagunta, M. S., Voss, J. C., & Persson, B. L. (2013). Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89. Biochemical and Biophysical Research Communications, 436(3), 551-556. https://doi.org/10.1016/j.bbrc.2013.06.011