ArticleProceedings of the National Academy of Sciences of the United States of America2008
Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 46 citations in OpenAlex.
- Regulation of potassium uptake inJournal of bacteriology · 2024Article
- Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans.Communications biology · 2023Article
- Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time.ACS central science · 2023Article
- GroEL Allostery Illuminated by a Relationship between the Hill Coefficient and the MWC Model.Biophysical journal · 2019Article
- Probing the mechanism of inhibition of amyloid-β(1-42)-induced neurotoxicity by the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Substrate protein dependence of GroEL-GroES interaction cycle revealed by high-speed atomic force microscopy imaging.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Article
- Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.Protein expression and purification · 2018Article
- Folding of maltose binding protein outside of and in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- GroEL actively stimulates folding of the endogenous substrate protein PepQ.Nature communications · 2017Article
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Using ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.Chembiochem : a European journal of chemical biology · 2014Article
- Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.The Journal of biological chemistry · 2013Article
- Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Putting handcuffs on the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Measuring how much work the chaperone GroEL can do.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The effects of potassium ion on the nested allostery of GroEL are due to increases in the affinity for nucleotide. Both positive allosteric transitions, TT-TR and TR-RR, occur at lower [ATP] as [K(+)] is increased. Negative cooperativity in the double-ringed system is also due to an increase in the affinity of the trans ring for the product ADP as [K(+)] is increased. Consequently, (i) rates of ATP hydrolysis are inversely proportional to [K(+)] and (ii) the residence time of GroES bound to the cis ring is prolonged and the hemicycle time extended. Substrate protein suppresses negative cooperativity by decreasing the affinity of the trans ring for ADP, reducing the hemicycle time to a constant minimum. The trans ring thus serves as a variable timer. ATP added to the asymmetric GroEL-GroES resting-state complex lacking trans ring ADP is hydrolyzed in the newly formed cis ring with a presteady-state burst of approximately 6 mol of Pi per mole of 14-mer. No burst is observed when the trans ring contains ADP. The amplitude and kinetics of ATP hydrolysis in the cis ring are independent of the presence or absence of encapsulated substrate protein and independent of K(+) at concentrations where there are profound effects on the linear steady-state rate. The hydrolysis of ATP by the cis ring constitutes a second, nonvariable timer of the chaperonin cycle.
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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.