ArticlePlant physiology2007
New insights into the unique structure of the F0F1-ATP synthase from the chlamydomonad algae Polytomella sp. and Chlamydomonas reinhardtii.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 58 citations in OpenAlex.
- Mitochondrial super complexes in the colorless chlorophycean alga Polytomella parva.Journal of bioenergetics and biomembranes · 2026Article
- Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025Article
- The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.Trends in parasitology · 2022Review
- Augmented CONature communications · 2021Article
- Supramolecular associations between atypical oxidative phosphorylation complexes of Euglena gracilis.Journal of bioenergetics and biomembranes · 2021Article
- Phylogenetic and functional diversity of aldehyde-alcohol dehydrogenases in microalgae.Plant molecular biology · 2021Article
- ATP synthase: Evolution, energetics, and membrane interactions.The Journal of general physiology · 2020Review
- Article
- ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid CytochromeFrontiers in plant science · 2017Article
- Unexpectedly Streamlined Mitochondrial Genome of the Euglenozoan Euglena gracilis.Genome biology and evolution · 2015Article
- Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking.The Journal of biological chemistry · 2015Article
- Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase.Nature · 2015Article
- ATPaseTb2, a unique membrane-bound FoF1-ATPase component, is essential in bloodstream and dyskinetoplastic trypanosomes.PLoS pathogens · 2015Article
- The Permeability Transition in Plant Mitochondria: The Missing Link.Frontiers in plant science · 2015Review
- Biochemical and structural studies of the large Ycf4-photosystem I assembly complex of the green alga Chlamydomonas reinhardtii.The Plant cell · 2009Article
- The fully-active and structurally-stable form of the mitochondrial ATP synthase of Polytomella sp. is dimeric.Journal of bioenergetics and biomembranes · 2009Article
- Bioenergetic consequences of FThe Journal of biological chemistryArticle
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we investigate the structure of the mitochondrial F(0)F(1)-ATP synthase of the colorless alga Polytomella sp. with respect to the enzyme of its green close relative Chlamydomonas reinhardtii. It is demonstrated that several unique features of the ATP synthase in C. reinhardtii are also present in Polytomella sp. The alpha- and beta-subunits of the ATP synthase from both algae are highly unusual in that they exhibit extensions at their N- and C-terminal ends, respectively. Several subunits of the Polytomella ATP synthase in the range of 9 to 66 kD have homologs in the green alga but do not have known equivalents as yet in mitochondrial ATP synthases of mammals, plants, or fungi. The largest of these so-called ASA (ATP Synthase-Associated) subunits, ASA1, is shown to be an extrinsic protein. Short heat treatment of isolated Polytomella mitochondria unexpectedly dissociated the otherwise highly stable ATP synthase dimer of 1,600 kD into subcomplexes of 800 and 400 kD, assigned as the ATP synthase monomer and F(1)-ATPase, respectively. Whereas no ASA subunits were found in the F(1)-ATPase, all but two were present in the monomer. ASA6 (12 kD) and ASA9 (9 kD), predicted to be membrane bound, were not detected in the monomer and are thus proposed to be involved in the formation or stabilization of the enzyme. A hypothetical configuration of the Chlamydomonad dimeric ATP synthase portraying its unique features is provided to spur further research on this topic.
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