Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89
(2013) In Biochemical and Biophysical Research Communications 436(3). p.551-556- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4053380
- author
- Sengottaiyan, Palanivelu ; Petrlova, Jitka LU ; Lagerstedt, Jens O LU ; Ruiz-Pavon, Lorena ; Budamagunta, Madhu S. ; Voss, John C LU and Persson, Bengt L
- organization
- publishing date
- 2013-07-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Pho89, Pichia pastoris, Oligomer, Reconstitution, Phosphate transport, Circular dichroism
- in
- Biochemical and Biophysical Research Communications
- volume
- 436
- issue
- 3
- pages
- 6 pages
- publisher
- Elsevier
- external identifiers
-
- wos:000321995900034
- scopus:84879889835
- pmid:23770362
- ISSN
- 1090-2104
- DOI
- 10.1016/j.bbrc.2013.06.011
- language
- English
- LU publication?
- yes
- id
- 9b9c4370-c17e-4c8e-9a91-7851f08534e1 (old id 4053380)
- date added to LUP
- 2016-04-01 13:34:14
- date last changed
- 2022-04-06 05:48:51
@article{9b9c4370-c17e-4c8e-9a91-7851f08534e1, abstract = {{<p>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.</p>}}, author = {{Sengottaiyan, Palanivelu and Petrlova, Jitka and Lagerstedt, Jens O and Ruiz-Pavon, Lorena and Budamagunta, Madhu S. and Voss, John C and Persson, Bengt L}}, issn = {{1090-2104}}, keywords = {{Pho89; Pichia pastoris; Oligomer; Reconstitution; Phosphate transport; Circular dichroism}}, language = {{eng}}, month = {{07}}, number = {{3}}, pages = {{551--556}}, publisher = {{Elsevier}}, series = {{Biochemical and Biophysical Research Communications}}, title = {{Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89}}, url = {{http://dx.doi.org/10.1016/j.bbrc.2013.06.011}}, doi = {{10.1016/j.bbrc.2013.06.011}}, volume = {{436}}, year = {{2013}}, }