The suppressor of AAC2 Lethality SAL1 modulates sensitivity of heterologously expressed artemia ADP/ATP carrier to bongkrekate in yeast
| Autor: | Lilla Turiák, Monika Wysocka-Kapcinska, Roza Kucharczyk, Andrea M. Hunt, Beáta Töröcsik, George Tsaprailis, Cynthia L. David, Christos Chinopoulos, Károly Vékey, Vera Adam-Vizi |
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| Rok vydání: | 2013 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Saccharomyces cerevisiae lcsh:Medicine Hemagglutinin (influenza) Mitochondrion 03 medical and health sciences Plasmid Adenosine Triphosphate Adenine nucleotide Drug Resistance Fungal Animals lcsh:Science 030304 developmental biology chemistry.chemical_classification 0303 health sciences Multidisciplinary biology lcsh:R 030302 biochemistry & molecular biology biology.organism_classification Molecular biology Yeast Amino acid Anti-Bacterial Agents Mitochondria Adenosine Diphosphate Biochemistry chemistry biology.protein lcsh:Q ATP–ADP translocase Artemia Bongkrekic Acid Mitochondrial ADP ATP Translocases Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 8, Iss 9, p e74187 (2013) |
| ISSN: | 1932-6203 |
| Popis: | The ADP/ATP carrier protein (AAC) expressed in Artemia franciscana is refractory to bongkrekate. We generated two strains of Saccharomyces cerevisiae where AAC1 and AAC3 were inactivated and the AAC2 isoform was replaced with Artemia AAC containing a hemagglutinin tag (ArAAC-HA). In one of the strains the suppressor of ΔAAC2 lethality, SAL1, was also inactivated but a plasmid coding for yeast AAC2 was included, because the ArAACΔsal1Δ strain was lethal. In both strains ArAAC-HA was expressed and correctly localized to the mitochondria. Peptide sequencing of ArAAC expressed in Artemia and that expressed in the modified yeasts revealed identical amino acid sequences. The isolated mitochondria from both modified strains developed 85% of the membrane potential attained by mitochondria of control strains, and addition of ADP yielded bongkrekate-sensitive depolarizations implying acquired sensitivity of ArAAC-mediated adenine nucleotide exchange to this poison, independent from SAL1. However, growth of ArAAC-expressing yeasts in glycerol-containing media was arrested by bongkrekate only in the presence of SAL1. We conclude that the mitochondrial environment of yeasts relying on respiratory growth conferred sensitivity of ArAAC to bongkrekate in a SAL1-dependent manner. |
| Databáze: | OpenAIRE |
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