Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.

PubWeight™: 1.67‹?› | Rank: Top 3%

🔗 View Article (PMC 3339572)

Published in Nat Struct Mol Biol on April 29, 2007

Authors

Stefanie Reissmann1, Charles Parnot, Christopher R Booth, Wah Chiu, Judith Frydman

Author Affiliations

1: Department of Biological Sciences and BioX Program, Stanford University, Stanford, California 94305, USA.

Articles citing this

Mechanism of folding chamber closure in a group II chaperonin. Nature (2010) 2.85

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci U S A (2010) 2.17

Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol (2008) 2.07

The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure (2012) 1.80

Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure (2011) 1.71

JADAS: a customizable automated data acquisition system and its application to ice-embedded single particles. J Struct Biol (2008) 1.62

Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol (2008) 1.51

A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol (2010) 1.41

Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling. Proc Natl Acad Sci U S A (2012) 1.36

The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT. Cell (2014) 1.31

Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. J Biol Chem (2010) 1.26

Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. Nat Struct Mol Biol (2010) 1.26

Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Cell (2011) 1.25

p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling. J Biol Chem (2009) 1.16

Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. EMBO J (2011) 1.12

A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Rep (2012) 0.97

Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution. Proc Natl Acad Sci U S A (2011) 0.97

Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT. Proc Natl Acad Sci U S A (2012) 0.95

xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry. Nat Methods (2015) 0.94

Probing single biomolecules in solution using the anti-Brownian electrokinetic (ABEL) trap. Acc Chem Res (2012) 0.94

The Mechanism and Function of Group II Chaperonins. J Mol Biol (2015) 0.93

Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers. J Biol Chem (2013) 0.91

Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins. J Biol Chem (2008) 0.91

Multiscale natural moves refine macromolecules using single-particle electron microscopy projection images. Proc Natl Acad Sci U S A (2012) 0.91

The group II chaperonin Mm-Cpn binds and refolds human γD crystallin. Protein Sci (2011) 0.90

Mechanism of nucleotide sensing in group II chaperonins. EMBO J (2011) 0.89

Hardware-based anti-Brownian electrokinetic trap (ABEL trap) for single molecules: Control loop simulations and application to ATP binding stoichiometry in multi-subunit enzymes. Proc SPIE Int Soc Opt Eng (2008) 0.87

Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress Chaperones (2012) 0.87

Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding. J Amino Acids (2011) 0.84

Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactor. J Biol Chem (2010) 0.82

Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy. J Biol Chem (2014) 0.82

ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. PLoS One (2013) 0.82

Archaeal-like chaperonins in bacteria. Proc Natl Acad Sci U S A (2010) 0.80

Contribution of the Type II Chaperonin, TRiC/CCT, to Oncogenesis. Int J Mol Sci (2015) 0.79

Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin. Structure (2016) 0.76

Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy. Sci Rep (2017) 0.75

Chaperonin-Dendrimer Conjugates for siRNA Delivery. Adv Sci (Weinh) (2016) 0.75

Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis. J Bacteriol (2016) 0.75

Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium. Nat Commun (2017) 0.75

The Human Mitochondrial Hsp60 in the APO Conformation Forms a Stable Tetradecameric Complex. Cell Cycle (2017) 0.75

Articles cited by this

SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res (2003) 25.86

The Hsp70 and Hsp60 chaperone machines. Cell (1998) 13.79

Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol (2004) 6.45

Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem (2001) 5.74

Structure and function in GroEL-mediated protein folding. Annu Rev Biochem (1998) 3.18

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol (2004) 3.18

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell (1998) 2.94

The changing landscape of protein allostery. Curr Opin Struct Biol (2006) 2.90

ATP-bound states of GroEL captured by cryo-electron microscopy. Cell (2001) 2.84

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell (1994) 2.84

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry (1995) 2.49

Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science (1996) 2.43

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell (1996) 2.28

Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell (2003) 2.02

GroEL-GroES-mediated protein folding. Chem Rev (2006) 1.98

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol (2006) 1.94

Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Mol Cell (2003) 1.66

Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol (2005) 1.62

Review: allostery in chaperonins. J Struct Biol (2001) 1.57

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. J Mol Biol (1999) 1.50

Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell (2006) 1.49

Specificity in chaperonin-mediated protein folding. Nature (1995) 1.47

Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms. J Mol Biol (2004) 1.46

Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry (1998) 1.26

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nat Struct Biol (1999) 1.19

Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1. Protein Sci (2001) 1.18

Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. J Mol Biol (2003) 1.14

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Adv Protein Chem (2001) 1.11

Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. J Biol Chem (2006) 1.09

Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis. Biochem J (2003) 1.07

Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae. J Mol Biol (2000) 1.06

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Nat Struct Mol Biol (2004) 1.05

Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin. J Mol Biol (2000) 1.04

Cooperativity in the thermosome. J Mol Biol (2005) 1.01

GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex. Biochemistry (1997) 1.01

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure. J Mol Biol (1996) 0.99

Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine". J Biol Chem (2005) 0.96

Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn. FEBS Lett (2003) 0.92

MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains. Protein Sci (1998) 0.91

The asymmetric ATPase cycle of the thermosome: elucidation of the binding, hydrolysis and product-release steps. J Mol Biol (2006) 0.91

Refolding of bovine mitochondrial rhodanese by chaperonins GroEL and GroES. Methods Mol Biol (2000) 0.83

Articles by these authors

Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat Methods (2013) 8.12

Misfolded proteins partition between two distinct quality control compartments. Nature (2008) 4.75

Outcome of the first electron microscopy validation task force meeting. Structure (2012) 4.35

Coupling ligand structure to specific conformational switches in the beta2-adrenoceptor. Nat Chem Biol (2006) 3.76

Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature (2006) 3.73

Paraneoplastic thrombocytosis in ovarian cancer. N Engl J Med (2012) 3.54

Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature (2008) 3.54

De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure (2008) 3.41

EMDataBank.org: unified data resource for CryoEM. Nucleic Acids Res (2010) 3.32

Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol (2004) 3.18

Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids. Nat Struct Mol Biol (2006) 3.14

Protein structure fitting and refinement guided by cryo-EM density. Structure (2008) 3.12

Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell (2007) 2.95

Refinement of protein structures into low-resolution density maps using rosetta. J Mol Biol (2009) 2.94

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell (2003) 2.89

Mechanism of folding chamber closure in a group II chaperonin. Nature (2010) 2.85

Systematic functional prioritization of protein posttranslational modifications. Cell (2012) 2.78

Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol (2003) 2.76

Interbilayer-crosslinked multilamellar vesicles as synthetic vaccines for potent humoral and cellular immune responses. Nat Mater (2011) 2.71

Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states. J Biol Chem (2003) 2.68

Common ancestry of herpesviruses and tailed DNA bacteriophages. J Virol (2005) 2.60

Identification of secondary structure elements in intermediate-resolution density maps. Structure (2007) 2.60

The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol (2006) 2.58

Remotely triggered liposome release by near-infrared light absorption via hollow gold nanoshells. J Am Chem Soc (2008) 2.56

Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell (2005) 2.55

Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy. Structure (2004) 2.50

Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J Struct Biol (2010) 2.48

The pore structure of the closed RyR1 channel. Structure (2005) 2.42

Outcome of a workshop on archiving structural models of biological macromolecules. Structure (2006) 2.32

Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell (2006) 2.30

Experimental verification of conformational variation of human fatty acid synthase as predicted by normal mode analysis. Structure (2004) 2.30

Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure (2006) 2.26

Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol (2005) 2.20

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci U S A (2010) 2.17

Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus. Nat Struct Mol Biol (2010) 2.12

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat Cell Biol (2013) 2.10

Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol (2008) 2.07

Refinement of protein structures by iterative comparative modeling and CryoEM density fitting. J Mol Biol (2006) 2.06

An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate. Structure (2006) 2.04

Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. PLoS Biol (2011) 2.04

Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc Natl Acad Sci U S A (2011) 2.03

Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell (2003) 2.02

The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat Struct Mol Biol (2009) 1.98

Direct electron detection yields cryo-EM reconstructions at resolutions beyond 3/4 Nyquist frequency. J Struct Biol (2012) 1.94

Structure of Halothiobacillus neapolitanus carboxysomes by cryo-electron tomography. J Mol Biol (2006) 1.90

Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. J Struct Biol (2007) 1.90

Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding. Nat Struct Mol Biol (2012) 1.87

Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev (2007) 1.87

The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure (2012) 1.80

DNA packaging and delivery machines in tailed bacteriophages. Curr Opin Struct Biol (2007) 1.79

A digital atlas to characterize the mouse brain transcriptome. PLoS Comput Biol (2005) 1.78

4.4 Å cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus. EMBO J (2011) 1.77

Principles of cotranslational ubiquitination and quality control at the ribosome. Mol Cell (2013) 1.76

Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol (2011) 1.74

Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure (2011) 1.71

Structure of a conserved retroviral RNA packaging element by NMR spectroscopy and cryo-electron tomography. J Mol Biol (2010) 1.71

A 9 angstroms single particle reconstruction from CCD captured images on a 200 kV electron cryomicroscope. J Struct Biol (2004) 1.70

Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel. Proc Natl Acad Sci U S A (2008) 1.68

Structural characterization of components of protein assemblies by comparative modeling and electron cryo-microscopy. J Struct Biol (2005) 1.67

Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Mol Cell (2003) 1.66

Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation. Mol Cell (2005) 1.65

JADAS: a customizable automated data acquisition system and its application to ice-embedded single particles. J Struct Biol (2008) 1.62

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Mol Cell Biol (2003) 1.62

Assessing the capabilities of a 4kx4k CCD camera for electron cryo-microscopy at 300kV. J Struct Biol (2006) 1.61

Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure (2010) 1.60

A monoclonal antibody for G protein-coupled receptor crystallography. Nat Methods (2007) 1.60

Structure of the acrosomal bundle. Nature (2004) 1.59

State of the science: an update on renal cell carcinoma. Mol Cancer Res (2012) 1.58

Cryo-EM of macromolecular assemblies at near-atomic resolution. Nat Protoc (2010) 1.58

Methods for aligning and for averaging 3D volumes with missing data. J Struct Biol (2007) 1.58

The role of mutational robustness in RNA virus evolution. Nat Rev Microbiol (2013) 1.54

A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform. Structure (2005) 1.53

The ribosome as a hub for protein quality control. Mol Cell (2013) 1.53

3D volume reconstruction of a mouse brain from histological sections using warp filtering. J Neurosci Methods (2006) 1.51

Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol (2008) 1.51

Applications of a bilateral denoising filter in biological electron microscopy. J Struct Biol (2003) 1.50

Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell (2006) 1.49

Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J Biol Chem (2004) 1.47

The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell (2013) 1.46

Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEM. Proc Natl Acad Sci U S A (2009) 1.45

A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol (2010) 1.41

Electron cryotomography reveals the portal in the herpesvirus capsid. J Virol (2006) 1.40

Three-dimensional architecture of the rod sensory cilium and its disruption in retinal neurodegeneration. Cell (2012) 1.40

Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J Biol Chem (2005) 1.39

Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine synechococcus. J Mol Biol (2007) 1.37

Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP. J Biol Chem (2003) 1.35

Automated segmentation of molecular subunits in electron cryomicroscopy density maps. J Struct Biol (2006) 1.34

Structure of the herpesvirus major capsid protein. EMBO J (2003) 1.33

Modeling protein structure at near atomic resolutions with Gorgon. J Struct Biol (2011) 1.29

Structure of Ca2+ release channel at 14 A resolution. J Mol Biol (2005) 1.27

Model of human low-density lipoprotein and bound receptor based on cryoEM. Proc Natl Acad Sci U S A (2009) 1.27

Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. J Biol Chem (2010) 1.26