Difference between revisions of "Havlickova 2010 Biochim Biophys Acta"
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{{Publication | {{Publication | ||
|title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J ( | |title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2010) Knockdown of F<sub>1</sub> epsilon subunit decreases mitochondrial content of ATP synthase 2 and leads to accumulation of subunit c. Biochim Biophys Acta 1797:1124-9. | ||
|authors= | |info=[http://www.ncbi.nlm.nih.gov/pubmed/20026007 PMID: 20026007 Open Access] | ||
|year= | |authors=Havlickova V, Kaplanova V, Nuskova H, Drahota Z, Houstek J | ||
|journal=Biochim | |year=2010 | ||
|abstract=The subunit ε of mitochondrial ATP synthase is the only | |journal=Biochim Biophys Acta | ||
|keywords=Mitochondria, | |abstract=The subunit ε of mitochondrial ATP synthase is the only F<sub>1</sub> subunit without a homolog in bacteria and chloroplasts and represents the least characterized F<sub>1</sub> subunit of the mammalian enzyme. Silencing of the ''ATP5E'' gene in HEK293 cells resulted in downregulation of the activity and content of the mitochondrial ATP synthase complex and of ADP-stimulated respiration to approximately 40% of the control. The decreased content of the ε subunit was paralleled by a decrease in the F<sub>1</sub> subunits α and β and in the F<sub>o</sub> subunits a and d while the content of the subunit c was not affected. The subunit c was present in the full-size ATP synthase complex and in subcomplexes of 200–400 kDa that neither contained the F<sub>1</sub> subunits, nor the F<sub>o</sub> subunits. The results indicate that the ε subunit is essential for the assembly of F<sub>1</sub> and plays an important role in the incorporation of the hydrophobic subunit c into the F<sub>1</sub>-c oligomer rotor of the mitochondrial ATP synthase complex. | ||
|keywords=Mitochondria, ATP synthase, Epsilon subunit, C subunit, Biogenesis | |||
|mipnetlab=CZ Prague Houstek J, CZ Hradec Kralove Cervinkova Z | |||
|discipline=Biomedicine | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration, mt-Biogenesis;mt-density, Genetic knockout;overexpression | |||
|enzymes=Complex V;ATP synthase | |||
|couplingstates=OXPHOS | |||
|instruments=Oxygraph-2k | |||
|discipline=Biomedicine | |discipline=Biomedicine | ||
}} | }} | ||
Latest revision as of 14:33, 20 May 2015
| Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2010) Knockdown of F1 epsilon subunit decreases mitochondrial content of ATP synthase 2 and leads to accumulation of subunit c. Biochim Biophys Acta 1797:1124-9. |
Havlickova V, Kaplanova V, Nuskova H, Drahota Z, Houstek J (2010) Biochim Biophys Acta
Abstract: The subunit ε of mitochondrial ATP synthase is the only F1 subunit without a homolog in bacteria and chloroplasts and represents the least characterized F1 subunit of the mammalian enzyme. Silencing of the ATP5E gene in HEK293 cells resulted in downregulation of the activity and content of the mitochondrial ATP synthase complex and of ADP-stimulated respiration to approximately 40% of the control. The decreased content of the ε subunit was paralleled by a decrease in the F1 subunits α and β and in the Fo subunits a and d while the content of the subunit c was not affected. The subunit c was present in the full-size ATP synthase complex and in subcomplexes of 200–400 kDa that neither contained the F1 subunits, nor the Fo subunits. The results indicate that the ε subunit is essential for the assembly of F1 and plays an important role in the incorporation of the hydrophobic subunit c into the F1-c oligomer rotor of the mitochondrial ATP synthase complex. • Keywords: Mitochondria, ATP synthase, Epsilon subunit, C subunit, Biogenesis
• O2k-Network Lab: CZ Prague Houstek J, CZ Hradec Kralove Cervinkova Z
Labels: MiParea: Respiration, mt-Biogenesis;mt-density, Genetic knockout;overexpression
Enzyme: Complex V;ATP synthase
Coupling state: OXPHOS
HRR: Oxygraph-2k
