The mitochondrial Oac (oxaloacetate carrier) found in some fungi and plants catalyses the uptake of oxaloacetate, malonate and sulfate. Despite their sequence similarity, transport specificity varies considerably between Oacs. Indeed, whereas ScOac (Saccharomyces cerevisiae Oac) is a specific anion–proton symporter, the YlOac (Yarrowia lipolytica Oac) has the added ability to transport protons, behaving as a UCP (uncoupling protein). Significantly, we identified two amino acid changes at the matrix gate of YlOac and ScOac, tyrosine to phenylalanine and methionine to leucine. We studied the role of these amino acids by expressing both wild-type and specifically mutated Oacs in an Oac-null S. cerevisiae strain. No phenotype could be associated with the methionine to leucine substitution, whereas UCP-like activity was dependent on the presence of the tyrosine residue normally expressed in the YlOac, i.e. Tyr-ScOac mediated proton transport, whereas Phe-YlOac lost its protonophoric activity. These findings indicate that the UCP-like activity of YlOac is determined by the tyrosine residue at position 146.
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Research Article|
March 14 2012
A critical tyrosine residue determines the uncoupling protein-like activity of the yeast mitochondrial oxaloacetate carrier
Luis A. Luévano-Martínez;
Luis A. Luévano-Martínez
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Carlos Barba-Ostria;
Carlos Barba-Ostria
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Daniela Araiza-Olivera;
Daniela Araiza-Olivera
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Natalia Chiquete-Félix;
Natalia Chiquete-Félix
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Sergio Guerrero-Castillo;
Sergio Guerrero-Castillo
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Eduardo Rial;
Eduardo Rial
†Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain
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Dimitris Georgellis;
Dimitris Georgellis
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
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Salvador Uribe-Carvajal
Salvador Uribe-Carvajal
1
*Department of Molecular Genetics, Instituto de Fisiología Celular, UNAM, México
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
June 06 2011
Revision Received:
January 03 2012
Accepted:
January 11 2012
Accepted Manuscript online:
January 11 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 443 (1): 317–325.
Article history
Received:
June 06 2011
Revision Received:
January 03 2012
Accepted:
January 11 2012
Accepted Manuscript online:
January 11 2012
Citation
Luis A. Luévano-Martínez, Carlos Barba-Ostria, Daniela Araiza-Olivera, Natalia Chiquete-Félix, Sergio Guerrero-Castillo, Eduardo Rial, Dimitris Georgellis, Salvador Uribe-Carvajal; A critical tyrosine residue determines the uncoupling protein-like activity of the yeast mitochondrial oxaloacetate carrier. Biochem J 1 April 2012; 443 (1): 317–325. doi: https://doi.org/10.1042/BJ20110992
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