ArticlePlant molecular biology2011
Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro.
Article in Plant molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- OsCpn60β1 is Essential for Chloroplast Development in Rice (International journal of molecular sciences · 2020Article
- Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018Review
- 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
- Article
- The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.PloS one · 2014Article
- The selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes.Frontiers in plant science · 2014Article
- OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL.Molecules and cells · 2013Article
- Article
- Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.The Journal of biological chemistry · 2012Article
- Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.PloS one · 2012Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The involvement of type I chaperonins in bacterial and organellar protein folding has been well-documented. In E. coli and mitochondria, these ubiquitous and highly conserved proteins form chaperonin oligomers of identical 60 kDa subunits (cpn60), while in chloroplasts, two distinct cpn60 α and β subunit types co-exist together. The primary sequence of α and β subunits is ~50% identical, similar to their respective homologies to the bacterial GroEL. Moreover, the A. thaliana genome contains two α and four β genes. The functional significance of this variability in plant chaperonin proteins has not yet been elucidated. In order to gain insight into the functional variety of the chloroplast chaperonin family members, we reconstituted β homo-oligomers from A. thaliana following their expression in bacteria and subjected them to a structure-function analysis. Our results show for the first time, that A. thaliana β homo-oligomers can function in vitro with authentic chloroplast co-chaperonins (ch-cpn10 and ch-cpn20). We also show that oligomers made up of different β subunit types have unique properties and different preferences for co-chaperonin partners. We propose that chloroplasts may contain active β homo-oligomers in addition to hetero-oligomers, possibly reflecting a variety of cellular roles.
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