ReviewPlant molecular biology2009
Cpn20: siamese twins of the chaperonin world.
Review in Plant molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 42 citations in OpenAlex.
- A temporal gradient of cytonuclear coordination of chaperonins and chaperones during RuBisCo biogenesis in allopolyploid plants.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The cryo-EM structure of the chloroplast ClpP complex.Nature plants · 2021Article
- Functional Exploration of Chaperonin (HSP60/10) Family Genes and their Abiotic Stress-induced Expression Patterns inCurrent genomics · 2021Article
- Reconstitution of Pure Chaperonin Hetero-Oligomer PreparationsFrontiers in molecular biosciences · 2018Article
- Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development.PLoS genetics · 2017Article
- Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis.Frontiers in molecular biosciences · 2017Review
- 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
- Cochaperonin CPN20 negatively regulates abscisic acid signaling in Arabidopsis.Plant molecular biology · 2013Article
- OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL.Molecules and cells · 2013Article
- Diversity in the origins of proteostasis networks--a driver for protein function in evolution.Nature reviews. Molecular cell biology · 2013Review
- Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD).Plant signaling & behavior · 2013Article
- Article
- Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.The Journal of biological chemistry · 2012Article
- Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro.Plant molecular biology · 2011Article
- A chaperonin subunit with unique structures is essential for folding of a specific substrate.PLoS biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chloroplast cpn20 protein is a functional homolog of the cpn10 co-chaperonin, but its gene consists of two cpn10-like units joined head-to-tail by a short chain of amino acids. This double protein is unique to plastids and was shown to exist in plants as well plastid-containing parasites. In vitro assays showed that this cpn20 co-chaperonin is a functional homolog of cpn10. In terms of structure, existing data indicate that the oligomer is tetrameric, yet it interacts with a heptameric cpn60 partner. Thus, the functional oligomeric structure remains a mystery. In this review, we summarize what is known about this distinctive chaperonin and use a bioinformatics approach to examine the expression of cpn20 in Arabidopsis thaliana relative to other chaperonin genes in this species. In addition, we examine the primary structure of the two homologous domains for similarities and differences, in comparison with cpn10 from other species. Lastly, we hypothesize as to the oligomeric structure and raison d'être of this unusual co-chaperonin homolog.
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Registered trials
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.