The substrate recognition mechanisms in chaperonins

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Journal of Molecular Recognition

• Publication date

  2004-03-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/JMR.654PMID 15027029
• 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.

• Allostery in chaperonins

  2006cited by this paper
• Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.

  2003cited by this paper
• Reversible Unfolding of FtsZ Cell Division Proteins from Archaea and Bacteria

  2002cited by this paper
• Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.

  2002cited by this paper
• Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT

  2002cited by this paper
• Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin.

  2002cited by this paper
• Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT

  2002cited by this paper
• Prokaryotic origin of the actin cytoskeleton

  2001cited by this paper
• Structural comparison of prokaryotic and eukaryotic chaperonins.

  2001cited by this paper
• Mutational screen identifies critical amino acid residues of beta-actin mediating interaction between its folding intermediates and eukaryotic cytosolic chaperonin CCT.

  2001cited by this paper
• ATP-induced structural change of the thermosome is temperature-dependent.

  2001cited by this paper
• Review: allostery in chaperonins.

  2001cited by this paper
• Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT.

  2001cited by this paper
• Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT.

  2001cited by this paper
• Gene duplication and the evolution of group II chaperonins: implications for structure and function.

  2001cited by this paper
• Type II chaperonins, prefoldin, and the tubulin-specific chaperones.

  2001cited by this paper
• The ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin‐assisted folding of actin and tubulin

  2001cited by this paper
• Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.

  2001cited by this paper
• Partial Occlusion of Both Cavities of the Eukaryotic Chaperonin with Antibody Has No Effect upon the Rates of β-Actin or α-Tubulin Folding*

  2000cited by this paper
• Defining the eukaryotic cytosolic chaperonin-binding sites in human tubulins.

  2000cited by this paper
• Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms.

  2000cited by this paper
• Evidence that beta-tubulin induces a conformation change in the cytosolic chaperonin which stabilizes binding: implications for the mechanism of action.

  2000cited by this paper
• Conformational rearrangements of an archaeal chaperonin upon ATPase cycling.

  2000cited by this paper
• Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding.

  2000cited by this paper
• Individual Subunits of the Eukaryotic Cytosolic Chaperonin Mediate Interactions with Binding Sites Located on Subdomains of β-Actin*

  2000cited by this paper
• Origin and evolution of eukaryotic chaperonins: phylogenetic evidence for ancient duplications in CCT genes.

  2000cited by this paper
• Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi‐native conformations

  2000cited by this paper
• Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin.

  2000influential reference
• Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae.

  2000influential reference
• Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

  2000cited by this paper
• The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity.

  1999cited by this paper
• Group II chaperonins: new TRiC(k)s and turns of a protein folding machine.

  1999influential reference
• 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

  1999cited by this paper
• Chaperonin function: folding by forced unfolding.

  1999cited by this paper
• The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins.

  1999influential reference
• Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.

  1999influential reference
• Identification of in vivo substrates of the chaperonin GroEL

  1999cited by this paper
• Principles of protein folding in the cellular environment.

  1999cited by this paper
• Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

  1999cited by this paper
• Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.

  1998cited by this paper
• Structure of the αβ tubulin dimer by electron crystallography

  1998influential reference
• Tubulin and FtsZ form a distinct family of GTPases

  1998influential reference
• A novel protein complex promoting formation of functional α‐ and γ‐tubulin

  1998cited by this paper
• Structure of the alpha beta tubulin dimer by electron crystallography.

  1998cited by this paper
• Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin.

  1998influential reference
• The Hsp70 and Hsp60 chaperone machines.

  1998cited by this paper
• This interaction seems to be largely independent of the structure or sequence of the substrate proteins

  1998cited by this paper
• Group II chaperonin in an open conformation examined by electron tomography

  1998influential reference
• ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex*

  1998cited by this paper
• The Chaperone Cofactor Hop/p60 Interacts with the Cytosolic Chaperonin-containing TCP-1 and Affects Its Nucleotide Exchange and Protein Folding Activities*

  1998cited by this paper
• Calorimetric Observation of a GroEL-Protein Binding Reaction with Little Contribution of Hydrophobic Interaction*

  1997cited by this paper
• The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

  1997influential reference
• A structural model for GroEL-polypeptide recognition.

  1997influential reference
• Structural and mechanistic consequences of polypeptide binding by GroEL.

  1997cited by this paper
• The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex.

  1997influential reference
• Electrostatic as well as hydrophobic interactions are important for the association of Cpn60 (groEL) with peptides

  1997cited by this paper
• Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.

  1997influential reference
• Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro‐complexes

  1997cited by this paper
• SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling

  1997cited by this paper
• Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL.

  1996cited by this paper
• Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity.

  1996cited by this paper
• Newly-synthesized beta-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin.

  1996influential reference
• Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL

  1996cited by this paper
• A thermodynamic coupling mechanism for GroEL-mediated unfolding.

  1996cited by this paper
• Chaperonin-mediated folding of actin and tubulin

  1996cited by this paper
• Nature and consequences of GroEL-protein interactions.

  1995cited by this paper
• Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

  1995cited by this paper
• Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding (*)

  1995cited by this paper
• Reversal by GroES of the GroEL Preference from Hydrophobic Amino Acids toward Hydrophilic Amino Acids (*)

  1995cited by this paper
• Prevention of in Vitro Protein Thermal Aggregation by the Sulfolobus solfataricus Chaperonin

  1995cited by this paper
• The Hydrophobic Nature of GroEL-Substrate Binding (*)

  1995cited by this paper
• Specificity in chaperonin-mediated protein folding

  1995influential reference
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

  1994influential reference
• Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.

  1994cited by this paper
• Amino acid specificity of the Escherichia coli chaperone GroEL (heat shock protein 60).

  1994cited by this paper
• Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin.

  1994cited by this paper
• Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry

  1994cited by this paper
• Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

  1994cited by this paper
• Residues in chaperonin GroEL required for polypeptide binding and release

  1994influential reference
• Molecular Chaperones: Opening and closing the Anfinsen cage

  1994cited by this paper
• Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo.

  1994cited by this paper
• Destabilization of the complete protein secondary structure on binding to the chaperone GroEL

  1994cited by this paper
• Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

  1994cited by this paper
• Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

  1994cited by this paper
• A polypeptide bound by the chaperonin groEL is localized within a central cavity.

  1993cited by this paper
• Protein structure comparison by alignment of distance matrices.

  1993influential reference
• Characterization of a functionally important mobile domain of GroES

  1993cited by this paper
• Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits.

  1993cited by this paper
• Different conformations for the same polypeptide bound to chaperones DnaK and GroEL

  1992cited by this paper
• TCP1 complex is a molecular chaperone in tubulin biogenesis

  1992cited by this paper
• Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits.

  1992influential reference
• A cytoplasmic chaperonin that catalyzes β-actin folding

  1992influential reference
• A cytoplasmic chaperonin that catalyzes beta-actin folding.

  1992influential reference
• T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

  1992cited by this paper
• The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.

  1991cited by this paper
• Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

  1991cited by this paper
• Binding of a chaperonin to the folding intermediates of lactate dehydrogenase.

  1991cited by this paper
• A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria.

  1991cited by this paper
• Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

  1991cited by this paper
• Atomic structure of the actin: DNase I complex

  1990cited by this paper

• Protein carbonylation reveals the molecular basis of cryoinjury in buffalo spermatozoa.

  2025cites this paper
• Chaperonin Mechanisms: Multiple and (Mis)Understood?

  2022cites this paper
• Upregulated YB-1 protein promotes glioblastoma growth through a YB-1/CCT4/mLST8/mTOR pathway

  2022cites this paper
• Sperm Functional Genome Associated With Bull Fertility

  2021cites this paper
• Schistosoma haematobium Extracellular Vesicle Proteins Confer Protection in a Heterologous Model of Schistosomiasis

  2020cites this paper
• A biotechnological approach to understanding the interactions between endothelial cell integrins and neuropilin-2 in angiogenesis

  2019cites this paper
• Structure and Function of the Cochaperone Prefoldin.

  2018cites this paper
• Common Patterns in Chaperone Interactions with a Native Client Protein.

  2018cites this paper
• Übereinstimmende Muster in Chaperon-Interaktionen mit einem nativen Klientenprotein

  2018cites this paper
• Expression study of fertility related genes with respect to sperm motility, HOST and acrosome integrity in bovine semen

  2018cites this paper
• Mechanism and Function of the Eukaryotic Chaperonin CCT

  2018cites this paper
• Thermosome: A Group II Chaperonin of Archaea

  2016cites this paper
• Extracellular vesicles secreted by highly metastatic clonal variants of osteosarcoma preferentially localize to the lungs and induce metastatic behaviour in poorly metastatic clones

  2016cites this paper
• Glucose-regulated protein 94 mediates metastasis by CCT8 and the JNK pathway in hepatocellular carcinoma

  2016cites this paper
• Protein quality control in the cytoplasm of yeast cells : substrate diversity and pathway selection

  2015cites this paper
• Dynamics, flexibility, and allostery in molecular chaperonins

  2015cites this paper
• TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells

  2014cites this paper
• Group II archaeal chaperonin recognition of partially folded human γD‐crystallin mutants

  2014cites this paper
• Functional analysis of Group 2 chaperonins from archaeal species in E. coli

  2014cites this paper
• Molecular determinants of the ATP hydrolysis asymmetry of the CCT chaperonin complex

  2014cites this paper
• Assembly and substrate recognition properties of human CCT subunits of the TRiC chaperonin

  2014cites this paper
• Rubredoxin refolding on nanostructured hydrophobic surfaces: Evidence for a new type of biomimetic chaperones

  2014cites this paper
• Chaperonin CCT-Mediated AIB1 Folding Promotes the Growth of ERα-Positive Breast Cancer Cells on Hard Substrates

  2014cites this paper
• Proteomic analysis of carbonylated proteins in the monkey substantia nigra after ischemia-reperfusion

  2014cites this paper
• Assisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteins

  2014cites this paper
• A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

  2014cites this paper
• Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

  2013cites this paper
• Interaction of p53 with the CCT Complex Promotes Protein Folding and Wild-Type p53 Activity

  2013cites this paper
• Proteomic profiling of differentially expressed proteins after exposure to asbestos

  2013cites this paper
• Structure of green type Rubisco activase from Nicotiana tabacum

  2012cites this paper
• Novel Phosducin-Like Protein Binding Partners: Exploring Chaperone and Tumor Suppressor Protein Interactions

  2012cites this paper
• The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa.

  2012cites this paper
• The molecular basis of sperm - oocyte interactions

  2012cites this paper
• Involvement of multimeric protein complexes in mediating the capacitation-dependent binding of human spermatozoa to homologous zonae pellucidae.

  2011cites this paper
• Functional Residues in Proteins

  2011cites this paper
• Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber.

  2011cites this paper
• Conformational dynamics of the molecular chaperone Hsp90

  2011cites this paper
• Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding

  2011cites this paper
• A phospho-proteomic screen identifies novel S6K1 and mTORC1 substrates revealing additional complexity in the signaling network regulating cell growth.

  2011cites this paper
• Towards proteome-on-a-chip : a new capillary electrophoresis based analytical platform with multiple read-out methods

  2011cites this paper
• Mechanism of G Protein Beta-Gamma Assembly Mediated by Phosducin-Like Protein 1

  2011cites this paper
• Chaperonins: two rings for folding.

  2011cites this paper
• CCTα and CCTδ Chaperonin Subunits Are Essential and Required for Cilia Assembly and Maintenance in Tetrahymena

  2010cites this paper
• The cytosolic fate of ricin A chain in target cells

  2010influential citation
• Plant‐extract‐induced changes in the proteome of the soil‐borne pathogenic fungus Thielaviopsis basicola

  2010cites this paper
• On the role of the chaperonin CCT in the just‐in‐time assembly process of APC/CCdc20

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• Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes.

  2010cites this paper
• Archaeal chaperonins.

  2009cites this paper
• Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei

  2009influential citation
• Structural dynamics and folding of beta-lactoglobulin probed by heteronuclear NMR.

  2009cites this paper
• Chaperones and protein folding in the archaea.

  2009cites this paper
• Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation.

  2008cites this paper
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  2008cites this paper
• [Heat shock proteins of the hyperthermophilic archaea].

  2008cites this paper
• Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae.

  2008cites this paper
• Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT

  2008cites this paper
• Thermal adaptation of heat shock proteins.

  2008cites this paper
• Bartonella Bacilliformis: Understanding The Underlying Causes Of Verruga Peruana Formation During Carrion’s Disease

  2008influential citation
• Chaperonins: The hunt for the Group II mechanism.

  2008cites this paper
• Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly-made proteins with complex topologies

  2008cites this paper
• Solution structure of the bb′ domains of human protein disulfide isomerase

  2008cites this paper
• Heat Shock Proteins: HSP60 Family Genes*

  2007cites this paper
• Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart.

  2007cites this paper
• The Role of Phosducin-like Protein as a Co-chaperone with the Cytosolic Chaperonin Complex in Assembly of the G Protein βγ Subunit Dimer

  2007cites this paper
• Promiscuous binding of ligands by beta-lactoglobulin involves hydrophobic interactions and plasticity.

  2007cites this paper
• All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable

  2006cites this paper
• Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins.

  2006influential citation
• Cytosolic chaperonins: a question of promiscuity.

  2006cites this paper
• GroEL-Mediated Protein Folding: Making the Impossible, Possible

  2006cites this paper
• Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands.

  2006cites this paper
• GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening.

  2006cites this paper
• Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring.

  2006cites this paper
• Cytosolic chaperonin protects folding intermediates of Gβ from aggregation by recognizing hydrophobic β-strands

  2006cites this paper
• Natural history as a predictor of protein evolvability.

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• Heat shock protein 10 and signal transduction: a “capsula eburnea” of carcinogenesis?

  2006cites this paper
• Immunochemical and proteomic analysis of covalent adducts formed by quinone methide tumor promoters in mouse lung epithelial cell lines.

  2005cites this paper
• Allosteric regulation of chaperonins.

  2005cites this paper
• A Novel, Evolutionarily Conserved Protein Phosphatase Complex Involved in Cisplatin Sensitivity*S

  2005cites this paper
• Folding, stability and polymerization properties of FtsZ chimeras with inserted tubulin loops involved in the interaction with the cytosolic chaperonin CCT and in microtubule formation.

  2005cites this paper
• Insights into Hydrophobicity and the Chaperone-like Function of αA- and αB-crystallins

  2005cites this paper
• Identifying natural substrates for chaperonins using a sequence‐based approach

  2005cites this paper
• Insights into hydrophobicity and the chaperone-like function of alphaA- and alphaB-crystallins: an isothermal titration calorimetric study.

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• Expression of mRNA for the t-complex polypeptide–1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua

  2005cites this paper
• Unfolding energetics of G-alpha-actin: a discrete intermediate can be re-folded to the native state by CCT.

  2005cites this paper
• Sequence and structural alignments of eukaryotic and prokaryotic cytoskeletal proteins

  2004cites this paper
• Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

  2004cites this paper