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Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89

Sengottaiyan, Palanivelu; Petrlova, Jitka LU ; Lagerstedt, Jens O LU ; Ruiz-Pavon, Lorena; Budamagunta, Madhu S.; Voss, John C LU and Persson, Bengt L (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:
author
organization
publishing date
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
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
2013-10-01 15:18:43
date last changed
2019-02-20 05:41:01
@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},
  keyword      = {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},
  volume       = {436},
  year         = {2013},
}