ArticleJournal of bacteriology2009
Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins.Communications biology · 2025Article
- Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2-mediated protein folding.Molecular microbiology · 2023Article
- Allosteric differences dictate GroEL complementation of E. coli.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Article
- Chaperonin Abundance Enhances Bacterial Fitness.Frontiers in molecular biosciences · 2021Article
- Article
- Comparative proteomic analysis of Xanthomonas citri ssp. citri periplasmic proteins reveals changes in cellular envelope metabolism during in vitro pathogenicity induction.Molecular plant pathology · 2018Article
- A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.Frontiers in molecular biosciences · 2018Review
- Ser/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation inNPJ biofilms and microbiomes · 2017Article
- GroEL2 of Mycobacterium tuberculosis Reveals the Importance of Structural Pliability in Chaperonin Function.Journal of bacteriology · 2016Article
- Phosphoproteomic analysis of the Chlamydia caviae elementary body and reticulate body forms.Microbiology (Reading, England) · 2015Article
- Multiple chaperonins in bacteria--novel functions and non-canonical behaviors.Cell stress & chaperones · 2015Review
- Mycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2.PLoS pathogens · 2014Article
- Enhanced translocation and growth of Rhodococcus erythropolis PR4 in the alkane phase of aqueous-alkane two phase cultures were mediated by GroEL2 overexpression.Microbes and environments · 2014Article
- Human resistin, a proinflammatory cytokine, shows chaperone-like activity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622.PLoS genetics · 2013Article
- Distinct features of protein folding by the GroEL system from a psychrophilic bacterium, Colwellia psychrerythraea 34H.Extremophiles : life under extreme conditions · 2012Article
- Bacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicity.Genomics, proteomics & bioinformatics · 2011Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The distinctive feature of the GroES-GroEL chaperonin system in mediating protein folding lies in its ability to exist in a tetradecameric state, form a central cavity, and encapsulate the substrate via the GroES lid. However, recombinant GroELs of Mycobacterium tuberculosis are unable to act as effective molecular chaperones when expressed in Escherichia coli. We demonstrate here that the inability of M. tuberculosis GroEL1 to act as a functional chaperone in E. coli can be alleviated by facilitated oligomerization. The results of directed evolution involving random DNA shuffling of the genes encoding M. tuberculosis GroEL homologues followed by selection for functional entities suggested that the loss of chaperoning ability of the recombinant mycobacterial GroEL1 and GroEL2 in E. coli might be due to their inability to form canonical tetradecamers. This was confirmed by the results of domain-swapping experiments that generated M. tuberculosis-E. coli chimeras bearing mutually exchanged equatorial domains, which revealed that E. coli GroEL loses its chaperonin activity due to alteration of its oligomerization capabilities and vice versa for M. tuberculosis GroEL1. Furthermore, studying the oligomerization status of native GroEL1 from cell lysates of M. tuberculosis revealed that it exists in multiple oligomeric forms, including single-ring and double-ring variants. Immunochemical and mass spectrometric studies of the native M. tuberculosis GroEL1 revealed that the tetradecameric form is phosphorylated on serine-393, while the heptameric form is not, indicating that the switch between the single- and double-ring variants is mediated by phosphorylation.
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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.