ArticlePlant physiology2014
The Arabidopsis protein CONSERVED ONLY IN THE GREEN LINEAGE160 promotes the assembly of the membranous part of the chloroplast ATP synthase.
Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- On the non-oxygenic origins of thylakoids.Communications biology · 2025Review
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Structure, function, and assembly of PSI in thylakoid membranes of vascular plants.The Plant cell · 2024Review
- Structure, Regulation, and Significance of Cyanobacterial and Chloroplast Adenosine Triphosphate Synthase in the Adaptability of Oxygenic Photosynthetic Organisms.Microorganisms · 2024Review
- Characterization of mutants deficient in N-terminal phosphorylation of the chloroplast ATP synthase subunit β.Plant physiology · 2023Article
- CGL160-mediated recruitment of the coupling factor CF1 is required for efficient thylakoid ATP synthase assembly, photosynthesis, and chloroplast development in Arabidopsis.The Plant cell · 2023Article
- De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome bNature communications · 2022Article
- PGRL2 triggers degradation of PGR5 in the absence of PGRL1.Nature communications · 2021Article
- NTRC Effects on Non-Photochemical Quenching Depends on PGR5.Antioxidants (Basel, Switzerland) · 2021Article
- HPlant physiology · 2020Article
- The Arabidopsis Protein CGL20 Is Required for Plastid 50S Ribosome Biogenesis.Plant physiology · 2020Article
- PPR Protein BFA2 Is Essential for the Accumulation of theFrontiers in plant science · 2019Article
- Does the stromal concentration of PPlant signaling & behavior · 2019Article
- Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.The Plant cell · 2018Article
- Chlorophyll Fluorescence Video Imaging: A Versatile Tool for Identifying Factors Related to Photosynthesis.Frontiers in plant science · 2018Review
- A Nucleus-Encoded Chloroplast Protein YL1 Is Involved in Chloroplast Development and Efficient Biogenesis of Chloroplast ATP Synthase in Rice.Scientific reports · 2016Article
- BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex.Plant physiology · 2016Article
- Recent advances in understanding photosynthesis.F1000Research · 2016Review
- PAB is an assembly chaperone that functions downstream of chaperonin 60 in the assembly of chloroplast ATP synthase coupling factor 1.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chloroplast F1Fo-ATP synthase/ATPase (cpATPase) couples ATP synthesis to the light-driven electrochemical proton gradient. The cpATPase is a multiprotein complex and consists of a membrane-spanning protein channel (comprising subunit types a, b, b', and c) and a peripheral domain (subunits α, β, γ, δ, and ε). We report the characterization of the Arabidopsis (Arabidopsis thaliana) CONSERVED ONLY IN THE GREEN LINEAGE160 (AtCGL160) protein (AtCGL160), conserved in green algae and plants. AtCGL160 is an integral thylakoid protein, and its carboxyl-terminal portion is distantly related to prokaryotic ATP SYNTHASE PROTEIN1 (Atp1/UncI) proteins that are thought to function in ATP synthase assembly. Plants without AtCGL160 display an increase in xanthophyll cycle activity and energy-dependent nonphotochemical quenching. These photosynthetic perturbations can be attributed to a severe reduction in cpATPase levels that result in increased acidification of the thylakoid lumen. AtCGL160 is not an integral cpATPase component but is specifically required for the efficient incorporation of the c-subunit into the cpATPase. AtCGL160, as well as a chimeric protein containing the amino-terminal part of AtCGL160 and Synechocystis sp. PCC6803 Atp1, physically interact with the c-subunit. We conclude that AtCGL160 and Atp1 facilitate the assembly of the membranous part of the cpATPase in their hosts, but loss of their functions provokes a unique compensatory response in each organism.
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