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

Palanivelu Sengottaiyan; Jitka Petrlova; Jens O. Lagerstedt; Lorena Ruiz-Pavon; Madhu S. Budamagunta; John C Voss; Bengt L. Persson

doi:10.1016/j.bbrc.2013.06.011

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

Palanivelu Sengottaiyan, Jitka Petrlova, Jens O. Lagerstedt, Lorena Ruiz-Pavon, Madhu S. Budamagunta, John C Voss, Bengt L. Persson

Biochemistry and Molecular Medicine

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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	https://doi.org/10.1016/j.bbrc.2013.06.011
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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Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89. / Sengottaiyan, Palanivelu; Petrlova, Jitka; Lagerstedt, Jens O.; Ruiz-Pavon, Lorena; Budamagunta, Madhu S.; Voss, John C; Persson, Bengt L.

In: Biochemical and Biophysical Research Communications, Vol. 436, No. 3, 05.07.2013, p. 551-556.

Research output: Contribution to journal › Article › peer-review

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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.",

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AU - Sengottaiyan, Palanivelu

AU - Petrlova, Jitka

AU - Lagerstedt, Jens O.

AU - Ruiz-Pavon, Lorena

AU - Budamagunta, Madhu S.

AU - Voss, John C

AU - Persson, Bengt L.

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AB - 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.

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