ArticleThe Journal of biological chemistry2014
Conversion of a chaperonin GroEL-independent protein into an obligate substrate.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed, 18 citations in OpenAlex.
- Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.Protein science : a publication of the Protein Society · 2024Article
- Article
- Prediction of chaperonin GroE substrates using small structural patterns of proteins.FEBS open bio · 2023Article
- Review
- Chaperonin Abundance Enhances Bacterial Fitness.Frontiers in molecular biosciences · 2021Article
- The substrate specificity of eukaryotic cytosolic chaperonin CCT.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Article
- Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity.Frontiers in molecular biosciences · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperones assist protein folding by preventing unproductive protein aggregation in the cell. In Escherichia coli, chaperonin GroEL/GroES (GroE) is the only indispensable chaperone and is absolutely required for the de novo folding of at least ∼60 proteins. We previously found that several orthologs of the obligate GroE substrates in Ureaplasma urealyticum, which lacks the groE gene in the genome, are E. coli GroE-independent folders, despite their significant sequence identities. Here, we investigated the key features that define the GroE dependence. Chimera or random mutagenesis analyses revealed that independent multiple point mutations, and even single mutations, were sufficient to confer GroE dependence on the Ureaplasma MetK. Strikingly, the GroE dependence was well correlated with the propensity to form protein aggregates during folding. The results reveal the delicate balance between GroE dependence and independence. The function of GroE to buffering the aggregation-prone mutations plays a role in maintaining higher genetic diversity of proteins.
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Registered trials
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