ArticleProceedings of the National Academy of Sciences of the United States of America2015
PAB is an assembly chaperone that functions downstream of chaperonin 60 in the assembly of chloroplast ATP synthase coupling factor 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 43 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
- Deciphering the regulatory network of carbon isotope discrimination in bread wheat through genome-wide association studies and genomic prediction.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Comparative Chloroplast Genomics ofInternational journal of molecular sciences · 2025Article
- Stress resilience inFrontiers in plant science · 2025Article
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Structure, Regulation, and Significance of Cyanobacterial and Chloroplast Adenosine Triphosphate Synthase in the Adaptability of Oxygenic Photosynthetic Organisms.Microorganisms · 2024Review
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- 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
- The tomato chloroplast stromal proteome compendium elucidated by leveraging a plastid protein-localization prediction Atlas.Frontiers in plant science · 2023Article
- Protective Responses at the Biochemical and Molecular Level Differ between aPlants (Basel, Switzerland) · 2022Article
- The plastid-encoded protein Orf2971 is required for protein translocation and chloroplast quality control.The Plant cell · 2022Article
- Chloroplast protease/chaperone AtDeg2 holds γPhotosynthetica · 2022Article
- Expression of a maize SOC1 gene enhances soybean yield potential through modulating plant growth and flowering.Scientific reports · 2021Article
- Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.Plant physiology · 2021Article
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- Light-inducedProceedings of the National Academy of Sciences of the United States of America · 2020Article
- F-Type ATP Synthase Assembly Factors Atp11 and Atp12 in Arabidopsis.Frontiers in plant science · 2020Article
- Integration of proteomic and genomic approaches to dissect seed germination vigor in Brassica napus seeds differing in oil content.BMC plant biology · 2019Article
- Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.The Plant cell · 2018Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chloroplast ATP synthase, a multisubunit complex in the thylakoid membrane, catalyzes the light-driven synthesis of ATP, thereby supplying the energy for carbon fixation during photosynthesis. The chloroplast ATP synthase is composed of both nucleus- and chloroplast-encoded proteins that have required the evolution of novel mechanisms to coordinate the biosynthesis and assembly of chloroplast ATP synthase subunits temporally and spatially. Here we have elucidated the assembly mechanism of the α3β3γ core complex of the chloroplast ATP synthase by identification and functional characterization of a key assembly factor, PAB (protein in chloroplast atpase biogenesis). PAB directly interacts with the nucleus-encoded γ subunit and functions downstream of chaperonin 60 (Cpn60)-mediated CF1γ subunit folding to promote its assembly into the catalytic core. PAB does not have any recognizable motifs or domains but is conserved in photosynthetic eukaryotes. It is likely that PAB evolved together with the transfer of chloroplast genes into the nucleus to assist nucleus-encoded CF1γ assembly into the CF1 core. Such coordination might represent an evolutionarily conserved mechanism for folding and assembly of nucleus-encoded proteins to ensure proper assembly of multiprotein photosynthetic complexes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.