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Phosphate permeases of Saccharomyces cerevisiae

B. L., Persson ; Berhe, A. ; Fristedt, U. ; Martinez, P. ; Pattison, J. ; Petersson, Jens LU and Weinander, R. (1998) In Biochimica et Biophysica Acta - Bioenergetics 1365(1-2). p.23-30
Abstract

The PHO84 and PHO89 genes of Saccharomyces cerevisiae encode two high- affinity phosphate cotransporters of the plasma membrane. Hydropathy analysis suggests a secondary structure arrangements of the proteins in 12 transmembrane domains. The derepressible Pho84 and Pho89 transporters appear to have characteristic similarities with the phosphate transporters of Neurospora crassa. The Pho84 protein catalyzes a proton-coupled phosphate transport at acidic pH, while the Pho89 protein catalyzes a sodium-dependent phosphate uptake at alkaline pH. The Pho84 transporter can be stably overproduced in the cytoplasmic membrane of Escherichia coli, purified and reconstituted in a functional state into proteoliposomes.

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author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
subject
keywords
PHO regulation, Phosphate transporter, Plasma membrane transport, Saccharomyces cerevisiae
in
Biochimica et Biophysica Acta - Bioenergetics
volume
1365
issue
1-2
pages
8 pages
publisher
Elsevier
external identifiers
  • scopus:0032320415
  • pmid:9693717
ISSN
0005-2728
DOI
10.1016/S0005-2728(98)00037-1
language
English
LU publication?
no
id
23fd7ec7-012d-43ec-adb6-e053943e2355
date added to LUP
2019-05-21 14:17:00
date last changed
2024-06-11 12:35:49
@article{23fd7ec7-012d-43ec-adb6-e053943e2355,
  abstract     = {{<p>The PHO84 and PHO89 genes of Saccharomyces cerevisiae encode two high- affinity phosphate cotransporters of the plasma membrane. Hydropathy analysis suggests a secondary structure arrangements of the proteins in 12 transmembrane domains. The derepressible Pho84 and Pho89 transporters appear to have characteristic similarities with the phosphate transporters of Neurospora crassa. The Pho84 protein catalyzes a proton-coupled phosphate transport at acidic pH, while the Pho89 protein catalyzes a sodium-dependent phosphate uptake at alkaline pH. The Pho84 transporter can be stably overproduced in the cytoplasmic membrane of Escherichia coli, purified and reconstituted in a functional state into proteoliposomes.</p>}},
  author       = {{B. L., Persson and Berhe, A. and Fristedt, U. and Martinez, P. and Pattison, J. and Petersson, Jens and Weinander, R.}},
  issn         = {{0005-2728}},
  keywords     = {{PHO regulation; Phosphate transporter; Plasma membrane transport; Saccharomyces cerevisiae}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{1-2}},
  pages        = {{23--30}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta - Bioenergetics}},
  title        = {{Phosphate permeases of Saccharomyces cerevisiae}},
  url          = {{http://dx.doi.org/10.1016/S0005-2728(98)00037-1}},
  doi          = {{10.1016/S0005-2728(98)00037-1}},
  volume       = {{1365}},
  year         = {{1998}},
}