Evidence for anion-translocating plant uncoupling mitochondrial protein in potato mitochondria
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
8955108
DOI
10.1074/jbc.271.51.32743
PII: S0021-9258(19)78773-0
Knihovny.cz E-resources
- MeSH
- Alkanesulfonates metabolism MeSH
- Anions metabolism MeSH
- Biological Transport MeSH
- Chlorides metabolism MeSH
- Intracellular Membranes physiology MeSH
- Ion Channels MeSH
- Hydrogen-Ion Concentration MeSH
- Fatty Acids metabolism MeSH
- Membrane Potentials MeSH
- Membrane Proteins metabolism MeSH
- Mitochondrial Proteins MeSH
- Mitochondria metabolism MeSH
- Oxidative Phosphorylation MeSH
- Uncoupling Agents MeSH
- Solubility MeSH
- Solanum tuberosum metabolism MeSH
- Carrier Proteins metabolism MeSH
- Uncoupling Protein 1 MeSH
- Mitochondrial Swelling MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Alkanesulfonates MeSH
- Anions MeSH
- Chlorides MeSH
- Ion Channels MeSH
- Fatty Acids MeSH
- Membrane Proteins MeSH
- Mitochondrial Proteins MeSH
- Uncoupling Agents MeSH
- Carrier Proteins MeSH
- Uncoupling Protein 1 MeSH
Transport properties of plant mitochondria from potato tubers were investigated using the swelling technique and membrane potential measurements. Proton-dependent swelling of fatty acid-depleted mitochondria in potassium acetate with valinomycin was possible only in the presence of fatty acids (linoleic acid and 12-(4-azido-2-nitrophenylamino)dodecanoic acid) and was inhibited by various purine nucleotides including ATP, GDP, and GTP. Swelling representing uptake of hexanesulfonate was also inhibited by purine nucleotides. Also, the membrane potential of fatty acid-depleted potato mitochondria energized by succinate declined upon the addition of linoleic acid or 12-(4-azido-2-nitrophenylamino)dodecanoic acid, and this decrease was prevented by ATP and other purine nucleotides. These transport activities are identical to those reported for brown adipose tissue mitochondria and related to the uncoupling protein; therefore, we ascribed them to the plant mitochondrial uncoupling protein (PUMP). A major difference between plant and mammalian uncoupling protein is that PUMP transports small hydrophilic anions such as Cl- very slowly, if at all. We suggest that PUMP may play an important role in plant physiology, where a regulated uncoupling and thermogenesis can proceed during fruit and seed development.
References provided by Crossref.org
Channel character of uncoupling protein-mediated transport