Crucial aminoacids in the FO sector of the F1FO-ATP synthase address H+ across the inner mitochondrial membrane: molecular implications in mitochondrial dysfunctions
| Autor: | Vittoria Ventrella, Cristina Algieri, Alessandra Pagliarani, Salvatore Nesci, Fabiana Trombetti |
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| Přispěvatelé: | Trombetti, Fabiana, Pagliarani, Alessandra, Ventrella, Vittoria, Algieri, Cristina, Nesci, Salvatore |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Mitochondrial disease Protein subunit Clinical Biochemistry Biochemistry F 1 F O -ATP synthase 03 medical and health sciences a Subunit medicine H + pathway Inner mitochondrial membrane Crucial aminoacid 030102 biochemistry & molecular biology ATP synthase biology Chemistry Point mutation Organic Chemistry Glutamate receptor medicine.disease Transmembrane protein 030104 developmental biology biology.protein Biophysics Mitochondrial dysfunction Flux (metabolism) |
| Zdroj: | Amino Acids. 51:579-587 |
| ISSN: | 1438-2199 0939-4451 |
| DOI: | 10.1007/s00726-019-02710-9 |
| Popis: | The eukaryotic F 1 F O -ATP synthase/hydrolase activity is coupled to H + translocation through the inner mitochondrial membrane. According to a recent model, two asymmetric H + half-channels in the a subunit translate a transmembrane vertical H + flux into the rotor rotation required for ATP synthesis/hydrolysis. Along the H + pathway, conserved aminoacid residues, mainly glutamate, address H + both in the downhill and uphill transmembrane movements to synthesize or hydrolyze ATP, respectively. Point mutations responsible for these aminoacid changes affect H + transfer through the membrane and, as a cascade, result in mitochondrial dysfunctions and related pathologies. The involvement of specific aminoacid residues in driving H + along their transmembrane pathway within a subunit, sustained by the literature and calculated data, leads to depict a model consistent with some mitochondrial disorders. |
| Databáze: | OpenAIRE |
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