ArticleProtein science : a publication of the Protein Society2006
Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans.Communications biology · 2023Article
- Signalling networks and dynamics of allosteric transitions in bacterial chaperonin GroEL: implications for iterative annealing of misfolded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- 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
- Putting handcuffs on the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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- Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Perturbation-based Markovian transmission model for probing allosteric dynamics of large macromolecular assembling: a study of GroEL-GroES.PLoS computational biology · 2009Article
- The GroEL/GroES cis cavity as a passive anti-aggregation device.FEBS letters · 2009Review
- Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks.Current protein & peptide science · 2009Article
- Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET.Journal of molecular biology · 2008Article
- Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations.Biophysical journal · 2007Article
- Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Dynamics of allosteric transitions in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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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
The ATPase activity of many types of molecular chaperones is stimulated by polypeptide substrate binding via molecular mechanisms that are, for the most part, unknown. Here, we report that such stimulation of the ATPase activity of GroEL is abolished when its conserved apical domain residue Glu257 is replaced by alanine. This mutation is also found to convert the ATPase profile of GroEL, a group I chaperonin, into one that is characteristic of group II chaperonins. Steady-state and transient kinetic analysis indicate that both effects are due, at least in part, to a reduction of the affinity of GroEL for ADP. This finding indicates that nonfolded proteins stimulate ATP hydrolysis by accelerating the off-rate of the ADP formed, thereby allowing more rapid cycles of ATP binding and hydrolysis.
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