Redundancy in the function of mitochondrial phosphate transport in Saccharomyces cerevisiae and Arabidopsis thaliana

Summary Most cellular ATP is produced within the mitochondria from ADP and Pi which are delivered across the inner‐membrane by specific nuclearly encoded polytopic carriers. In Saccharomyces cerevisiae, some of these carriers and in particular the ADP/ATP carrier, are represented by several related...

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Bibliographic Details
Published in:Molecular microbiology 2004-01, Vol.51 (2), p.307-317
Main Authors: Hamel, Patrice, Saint‐Georges, Yann, De Pinto, Brigida, Lachacinski, Nicole, Altamura, Nicola, Dujardin, Geneviève
Format: Article
Language:English
Subjects:
Adenosine Diphosphate - metabolism
Adenosine Triphosphate - metabolism
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis thaliana
Base Sequence
Biochemistry, Molecular Biology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Life Sciences
Microbiology
Miscellaneous
Mitochondria - genetics
Mitochondria - metabolism
Mycology
Open Reading Frames
phosphate
Phosphate Transport Proteins - genetics
Phosphate Transport Proteins - isolation & purification
PIC2 gene
Pic2 protein
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
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Summary:Summary Most cellular ATP is produced within the mitochondria from ADP and Pi which are delivered across the inner‐membrane by specific nuclearly encoded polytopic carriers. In Saccharomyces cerevisiae, some of these carriers and in particular the ADP/ATP carrier, are represented by several related isoforms that are distinct in their pattern of expression. Until now, only one mitochondrial Pi carrier (mPic) form, encoded by the MIR1 gene in S. cerevisiae, has been described. Here we show that the gene product encoded by the YER053C ORF also participates in the delivery of phosphate to the mitochondria. We have called this gene PIC2 for Pi carrier isoform 2. Overexpression of PIC2 compensates for the mitochondrial defect of the double mutant Δmir1 Δpic2 and restores phosphate transport activity in mitochondria swelling experiments. The existence of two isoforms of mPic does not seem to be restricted to S. cerevisiae as two Arabidopsis thaliana cDNAs encoding two different mPic‐like proteins are also able to complement the double mutant Δmir1 Δpic2. Finally, we demonstrate that Pic2p is a mitochondrial protein and that its steady state level increases at high temperature. We propose that Pic2p is a minor form of mPic which plays a role under specific stress conditions.
ISSN:0950-382X
1365-2958
DOI:10.1046/j.1365-2958.2003.03810.x