ArticleCell stress & chaperones2007
Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalent.
Article in Cell stress & chaperones, 2007. 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, 28 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Allosteric differences dictate GroEL complementation of E. coli.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Article
- A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.Frontiers in molecular biosciences · 2018Review
- Article
- Multiple chaperonins in bacteria--novel functions and non-canonical behaviors.Cell stress & chaperones · 2015Review
- Global transcriptional response to heat shock of the legume symbiont Mesorhizobium loti MAFF303099 comprises extensive gene downregulation.DNA research : an international journal for rapid publication of reports on genes and genomes · 2014Article
- Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.BMC evolutionary biology · 2013Article
- OsCpn60α1, encoding the plastid chaperonin 60α subunit, is essential for folding of rbcL.Molecules and cells · 2013Article
- Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622.PLoS genetics · 2013Article
- A chaperonin subunit with unique structures is essential for folding of a specific substrate.PLoS biology · 2011Article
- Myxococcus xanthus viability depends on groEL supplied by either of two genes, but the paralogs have different functions during heat shock, predation, and development.Journal of bacteriology · 2010Article
- Cpn20: siamese twins of the chaperonin world.Plant molecular biology · 2009Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many bacteria possess 2 or more genes for the chaperonin GroEL and the cochaperonin GroES. In particular, rhizobial species often have multiple groEL and groES genes, with a high degree of amino-acid similarity, in their genomes. The Rhizobium leguminosarum strain A34 has 3 complete groE operons, which we have named cpn.1, cpn.2 and cpn.3. Previously we have shown the cpn. 1 operon to be essential for growth, but the two other cpn operons to be dispensable. Here, we have investigated the extent to which loss of the essential GroEL homologue Cpn60.1 can be compensated for by expression of the other two GroEL homologues (Cnp60.2 and Cpn60.3). Cpn60.2 could not be overexpressed to high levels in R. leguminosarum, and was unable to replace Cpn60.1. A strain that overexpressed Cpn60.3 grew in the absence of Cpn60.1, but the complemented strain displayed a temperature-sensitive phenotype. Cpn60.1 and Cpn60.3, when coexpressed in Escherichia coli, preferentially selfassembled rather than forming mixed heteroligomers. We conclude that, despite their high amino acid similarity, the GroEL homologues of R. leguminosarum are not functionally equivalent in vivo.
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