Assembly-dependent translation of subunits 6 (Atp6) and 9 (Atp9) of ATP synthase in yeast mitochondria. Issue 3 (20th January 2022)
- Record Type:
- Journal Article
- Title:
- Assembly-dependent translation of subunits 6 (Atp6) and 9 (Atp9) of ATP synthase in yeast mitochondria. Issue 3 (20th January 2022)
- Main Title:
- Assembly-dependent translation of subunits 6 (Atp6) and 9 (Atp9) of ATP synthase in yeast mitochondria
- Authors:
- Kabala, Anna M
Binko, Krystyna
Godard, François
Charles, Camille
Dautant, Alain
Baranowska, Emilia
Skoczen, Natalia
Gombeau, Kewin
Bouhier, Marine
Becker, Hubert D
Ackerman, Sharon H
Steinmetz, Lars M
Tribouillard-Tanvier, Déborah
Kucharczyk, Roza
di Rago, Jean-Paul - Editors:
- Mitchell, A
- Abstract:
- Abstract: The yeast mitochondrial ATP synthase is an assembly of 28 subunits of 17 types of which 3 (subunits 6, 8, and 9 ) are encoded by mitochondrial genes, while the 14 others have a nuclear genetic origin. Within the membrane domain (FO ) of this enzyme, the subunit 6 and a ring of 10 identical subunits 9 transport protons across the mitochondrial inner membrane coupled to ATP synthesis in the extra-membrane structure (F1 ) of ATP synthase. As a result of their dual genetic origin, the ATP synthase subunits are synthesized in the cytosol and inside the mitochondrion. How they are produced in the proper stoichiometry from two different cellular compartments is still poorly understood. The experiments herein reported show that the rate of translation of the subunits 9 and 6 is enhanced in strains with mutations leading to specific defects in the assembly of these proteins. These translation modifications involve assembly intermediates interacting with subunits 6 and 9 within the final enzyme and cis -regulatory sequences that control gene expression in the organelle. In addition to enabling a balanced output of the ATP synthase subunits, these assembly-dependent feedback loops are presumably important to limit the accumulation of harmful assembly intermediates that have the potential to dissipate the mitochondrial membrane electrical potential and the main source of chemical energy of the cell.
- Is Part Of:
- Genetics. Volume 220:Issue 3(2022)
- Journal:
- Genetics
- Issue:
- Volume 220:Issue 3(2022)
- Issue Display:
- Volume 220, Issue 3 (2022)
- Year:
- 2022
- Volume:
- 220
- Issue:
- 3
- Issue Sort Value:
- 2022-0220-0003-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-01-20
- Subjects:
- ATP synthase -- mitochondria -- mitochondrial biogenesis -- mitochondria DNA -- yeast -- mitochondrial gene expression
Genetics -- Periodicals
576.5 - Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1093/genetics/iyac007 ↗
- Languages:
- English
- ISSNs:
- 0016-6731
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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- 25782.xml