Modular assembly of yeast mitochondrial ATP synthase
Open accessAbstract
The mitochondrial ATP synthase (F(1)-F(0) complex) of Saccharomces cerevisiae is a composite of different structural and functional units that jointly couple ATP synthesis and hydrolysis to proton transfer across the inner membrane. In organello, pulse labelling and pulse-chase experiments have enabled us to track the mitochondrially encoded Atp6p, Atp8p and Atp9p subunits of F(0) and to identify different assembly intermediates into which they are assimilated. Surprisingly, these core subunits of F(0) segregated into two different assembly intermediates one of which is composed of Atp6p, Atp8p, at least two stator subunits, and the Atp10p chaperone while the second consists of the F(1) ATPase and Atp9p ring. These studies show that assembly of the ATP synthase is not a single linear process, as previously thought, but rather involves two separate but coordinately regulated pathways that converge at the end stage.
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Mitochondrial proteins, such as ATP synthases, are thought to be preferentially translated near the organelle.
“Mitochondrial proteins, such as ATP synthases, are thought to be preferentially translated near the organelle (Margeot et al, 2005; Smits et al, 2010; Rak et al, 2011)”
From Differential dynamics of the mammalian mRNA and protein expression response to misfolding stress (2016) · cites this paper as Rak et al, 2011
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Differential dynamics of the mammalian mRNA and protein expression response to misfolding stress
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- Authors
- Rak, M., Gokova, S., & Tzagoloff, A.
- Affiliations
- Columbia University (US)
- Corresponding author
- Tzagoloff, Alexander
- Venue
- The EMBO Journal
- Published
- 2011-01-25
- Volume
- 30
- Issue
- 5
- Pages
- 920-930
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3049208
- OpenAlex
- W1835382900
- Cited by
- 106
- References
- 35
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 9 · 2019: 3 · 2018: 12 · 2017: 8 · 2016: 8 · 2015: 12 · 2014: 8 · 2013: 9 · 2012: 13
- FWCI
- 4.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL22174, R01HL022174, R56HL022174)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- mitochondrial ATP synthase, subunit assembly, assembly intermediates, F1-ATPase, Saccharomyces cerevisiae, pulse-chase labeling
- MeSH terms
- DNA, Fungal, DNA, Mitochondrial, Proton-Translocating ATPases, Mitochondria, Saccharomyces cerevisiae, Immunoblotting, Polymerase Chain Reaction, Molecular Chaperones, Protein Subunits, Mitochondrial Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins
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