ArticleThe Journal of biological chemistry2012
Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.
Article in The Journal of biological chemistry, 2012. 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, 53 citations in OpenAlex.
- Review
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- The cryo-EM structure of the chloroplast ClpP complex.Nature plants · 2021Article
- Proteostatic Regulation of MEP and Shikimate Pathways by Redox-Activated Photosynthesis Signaling in Plants Exposed to Small Fungal Volatiles.Frontiers in plant science · 2021Article
- Chlorophyll a Fluorescence Transient and 2-Dimensional Electrophoresis Analyses Reveal Response Characteristics of Photosynthesis to Heat Stress inPlants (Basel, Switzerland) · 2020Article
- Interrogating Membrane Protein Structure and Lipid Interactions by Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Red algal Rubisco fails to accumulate in transplastomic tobacco expressingPlant direct · 2018Article
- An improvedThe Journal of biological chemistry · 2018Article
- Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018Review
- A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.Frontiers in molecular biosciences · 2018Review
- Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis.Frontiers in molecular biosciences · 2017Review
- Article
- Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2 Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved in Regulating Histone Transcription.The Journal of biological chemistry · 2015Article
- Improving recombinant Rubisco biogenesis, plant photosynthesis and growth by coexpressing its ancillary RAF1 chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Opposing effects of folding and assembly chaperones on evolvability of Rubisco.Nature chemical biology · 2015Article
- Role of small subunit in mediating assembly of red-type form I Rubisco.The Journal of biological chemistry · 2015Article
- The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.PloS one · 2014Article
- Effect of r-Mt-Cpn10 on human osteoblast cells.International journal of clinical and experimental medicine · 2014Article
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5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chloroplast chaperonin system of plants and green algae is a curiosity as both the chaperonin cage and its lid are encoded by multiple genes, in contrast to the single genes encoding the two components of the bacterial and mitochondrial systems. In the green alga Chlamydomonas reinhardtii (Cr), three genes encode chaperonin cofactors, with cpn10 encoding a single ∼10-kDa domain and cpn20 and cpn23 encoding tandem cpn10 domains. Here, we characterized the functional interaction of these proteins with the Escherichia coli chaperonin, GroEL, which normally cooperates with GroES, a heptamer of ∼10-kDa subunits. The C. reinhardtii cofactor proteins alone were all unable to assist GroEL-mediated refolding of bacterial ribulose-bisphosphate carboxylase/oxygenase but gained this ability when CrCpn20 and/or CrCpn23 was combined with CrCpn10. Native mass spectrometry indicated the formation of hetero-oligomeric species, consisting of seven ∼10-kDa domains. The cofactor "heptamers" interacted with GroEL and encapsulated substrate protein in a nucleotide-dependent manner. Different hetero-oligomer arrangements, generated by constructing cofactor concatamers, indicated a preferential heptamer configuration for the functional CrCpn10-CrCpn23 complex. Formation of heptamer Cpn10/Cpn20 hetero-oligomers was also observed with the Arabidopsis thaliana (At) cofactors, which functioned with the chloroplast chaperonin, AtCpn60α(7)β(7). It appears that hetero-oligomer formation occurs more generally for chloroplast chaperonin cofactors, perhaps adapting the chaperonin system for the folding of specific client proteins.
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