(Mg–ATP)-dependent self-assembly of molecular chaperone GroEL

No abstract is available for this paper.

• Publication year

  1990

• Venue

  Nature

• Publication date

  1990-11-22

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1038/348339A0PMID 1979147
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta‐lactamase precursor.

  1990cited by this paper
• Demonstration by genetic suppression of interaction of GroE products with many proteins

  1989cited by this paper
• Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

  1989cited by this paper
• GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

  1989cited by this paper
• Thermodynamic Problems of Protein Structure

  1989cited by this paper
• Three pure chaperone proteins of Escherichia coli‐‐SecB, trigger factor and GroEL‐‐form soluble complexes with precursor proteins in vitro.

  1989cited by this paper
• Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides.

  1989cited by this paper
• Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures.

  1989cited by this paper
• Thermodynamic problems of protein structure.

  1989cited by this paper
• Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells.

  1989cited by this paper
• Homologous plant and bacterial proteins chaperone oligomeric protein assembly

  1988cited by this paper
• Stability of protein structure and hydrophobic interaction.

  1988cited by this paper
• Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein

  1988cited by this paper
• Proteins as molecular chaperones

  1987cited by this paper
• Purification and properties of the groES morphogenetic protein of Escherichia coli.

  1986cited by this paper
• Speculations on the functions of the major heat shock and glucose-regulated proteins.

  1986cited by this paper
• Interactions of bacteriophage and host macromolecules in the growth of bacteriophage lambda.

  1984cited by this paper
• Electrophoresis buffers for polyacrylamide gels at various pH.

  1982cited by this paper
• Estimation of globular protein secondary structure from circular dichroism.

  1981cited by this paper
• Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly.

  1979cited by this paper
• Purification and properties of groE, a host protein involved in bacteriophage assembly.

  1979cited by this paper
• A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. II. Enzymatic properties and molecular structure.

  1976cited by this paper
• A rapid micromethod for the determination of nitrogen and phosphate in biological material.

  1974cited by this paper

• New moonlighting activities for various GroEL/Hsp60 proteins, mainly characterized using recombinant M. tuberculosis GroEL1.

  2025cites this paper
• New Swiss-knife activities of GroEL/Hsp60 proteins

  2025cites this paper
• Co-chaperonin GroES subunit exchange as dependent on time, pH, protein concentration, and urea.

  2024cites this paper
• In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties

  2023cites this paper
• Influence of Chaperones on Amyloid Formation of Аβ Peptide.

  2022cites this paper
• Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP), and Stoichiometry of GroEL-GroES Complexes.

  2021cites this paper
• Novel cryo-EM structure of an ADP-bound GroEL–GroES complex

  2021cites this paper
• Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

  2020cites this paper
• A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis

  2020cites this paper
• Chaperonin-assisted protein folding: a chronologue

  2020cites this paper
• Investigating the function of GroES with hard-to-fold proteins in vivo

  2019cites this paper
• The molecular chaperone GroEL in complex with denatured proteins: increasing stability against temperature and trypsin action

  2018cites this paper
• Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.

  2018cites this paper
• [Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro].

  2018cites this paper
• Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy

  2018cites this paper
• Basic Biological Anticipation

  2017cites this paper
• Cooperative Subunit Refolding of a Light-Harvesting Protein through a Self-Chaperone Mechanism.

  2017cites this paper
• GroEL and the GroEL-GroES Complex.

  2017cites this paper
• Folding and unfolding pathway of chaperonin GroEL monomer and elucidation of thermodynamic parameters.

  2017cites this paper
• Dataset concerning GroEL chaperonin interaction with proteins

  2016cites this paper
• Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin.

  2016cites this paper
• GroEL/ES Chaperonin: Unfolding and Refolding Reactions

  2016cites this paper
• Protomer Roles in Chloroplast Chaperonin Assembly and Function.

  2015cites this paper
• Separation of E. coli chaperonin groEL from β-galactosidase without denaturation.

  2015cites this paper
• Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

  2014influential citation
• Picornavirus assembly in recombinant systems

  2014cites this paper
• Molecular chaperone GroEL/ES: Unfolding and refolding processes

  2013cites this paper
• Towards Functional Orthogonalisation of Protein Complexes: Individualisation of GroEL Monomers Leads to Distinct Quasihomogeneous Single Rings

  2013cites this paper
• Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL

  2013cites this paper
• The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function

  2012cites this paper
• Conformational Sampling and Nucleotide-Dependent Transitions of the GroEL Subunit Probed by Unbiased Molecular Dynamics Simulations

  2011cites this paper
• Physiological responses of Escherichia coli exposed to different heat-stress kinetics

  2010cites this paper
• Biporous polymeric beads fabricated by double emulsification for high‐speed protein chromatography

  2007cites this paper
• Affinity chromatography of GroEL chaperonin based on denatured proteins: Role of electrostatic interactions in regulation of GroEL affinity for protein substrates

  2006cites this paper
• Reconstitution and function of Tetragenococcus halophila chaperonin 60 tetradecamer.

  2005cites this paper
• Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins.

  2004cites this paper
• Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese.

  2004cites this paper
• [The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure].

  2004cites this paper
• Denaturation and reassembly of chaperonin GroEL studied by solution X‐ray scattering

  2003cites this paper
• The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure

  2003cites this paper
• Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities.

  2003cites this paper
• Excluded Volume Effects on the Refolding and Assembly of an Oligomeric Protein

  2001cites this paper
• Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1.

  2001cites this paper
• Assembly of chaperonin complexes

  2001influential citation
• Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain.

  2000cites this paper
• Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding*

  2000cites this paper
• Assembly and disassembly of GroEL and GroES complexes.

  2000cites this paper
• GroES co‐chaperonin small‐angle X‐ray scattering study shows ring orifice increase in solution

  2000cites this paper
• Removing trace fluorescent contaminants from GroEL preparations.

  2000cites this paper
• High Salt-induced Conversion of Escherichia coliGroEL into a Fully Functional Thermophilic Chaperonin*

  2000cites this paper
• Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model.

  1999cites this paper
• Refolding of pyridoxine-5'-P oxidase assisted by GroEL.

  1999cites this paper
• [Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization].

  1999cites this paper
• Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers.

  1998cites this paper
• DnaK-dependent ribosome biogenesis in Escherichia coli : competition for dominance between the alleles dnaK756 and dnaK +

  1998cites this paper
• Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase.

  1998cites this paper
• Structural perturbation of α-crystallin and its chaperone-like activity

  1998cites this paper
• Structural perturbation of alpha-crystallin and its chaperone-like activity.

  1998cites this paper
• [Denatured transitions of the molecular chaperone GroEL from Escherichia coli].

  1997cites this paper
• Molecular clues to pathogenesis in prion diseases.

  1997cites this paper
• GroES binding regulates GroEL chaperonin activity under heat shock

  1997cites this paper
• The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype.

  1997cites this paper
• Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate.

  1997cites this paper
• Ligands regulate GroEL thermostability

  1997cites this paper
• GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

  1997cites this paper
• Phosphofructokinase interacts with molecular chaperonins GroEL and GroES

  1997cites this paper
• Atomic force microscopy visualizes ATP-dependent dissociation of multimeric TATA-binding protein before translocation into the cell nucleus

  1996cites this paper
• Molecular chaperones and protein folding in plants

  1996cites this paper
• Reversible oligomerization and denaturation of the chaperonin GroES.

  1996cites this paper
• The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures.

  1996cites this paper
• Autocatalytic Folding of the Folding Catalyst FKBP12*

  1996cites this paper
• Regulation of Chaperonin Gene Expression

  1996cites this paper
• 3 – Chaperonins of Photosynthetic Organisms

  1996cites this paper
• Protein folding in the central cavity of the GroEL–GroES chaperonin complex

  1996cites this paper
• Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization.

  1995cites this paper
• A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone (*)

  1995cites this paper
• Molecular chaperones and intracellular protein translocation.

  1995cites this paper
• In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATP

  1995cites this paper
• Residual structure in urea-denatured chaperonin GroEL.

  1995cites this paper
• Stability of the Asymmetric Escherichia coli Chaperonin Complex

  1995cites this paper
• Spinach Chloroplast cpn21 Co-chaperonin Possesses Two Functional Domains Fused Together in a Toroidal Structure and Exhibits Nucleotide-dependent Binding to Plastid Chaperonin 60 (*)

  1995cites this paper
• Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins.

  1995cites this paper
• Refolding and Reassembly of Active Chaperonin GroEL After Denaturation (*)

  1995cites this paper
• Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.

  1995cites this paper
• Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent.

  1995cites this paper
• Direct demonstration that ATP is in contact with Cys-137 in chaperonin GroEL.

  1994cites this paper
• The tail of a chaperonin: the C‐terminal region of Esctierichia coli GroEL protein

  1994cites this paper
• Chaperonins and Protein Folding

  1994cites this paper
• Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

  1994cites this paper
• Isolation and characterization of a chaperonin-60 gene of the human malaria parasite Plasmodium falciparum.

  1994cites this paper
• The guanidine-induced conformational changes of the chaperonin GroEL from Escherichia coli. Evidence for the existence of an unfolding intermediate state.

  1994cites this paper
• Heat-shock proteins as molecular chaperones.

  1994cites this paper
• Structural and Functional Aspects of Chaperonin-Mediated Protein Folding

  1994cites this paper
• The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518.

  1994cites this paper
• Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

  1994cites this paper
• On the role of groES in the chaperonin-assisted folding reaction. Three case studies.

  1994cites this paper
• Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding.

  1994cites this paper
• The Biochemistry and Molecular Regulation of Carbon Dioxide Metabolism in Cyanobacteria

  1994cites this paper
• Identification, Cellular Localization, and Participation of Chaperonins in Protein Folding

  1994cites this paper
• GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms.

  1994cites this paper