Recombinant protein folding and misfolding in Escherichia coli

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Nature Biotechnology

• Publication date

  2004-11-01

• Fields of study

  Biology, Medicine, Chemistry, Engineering

• Identifiers
  DOI 10.1038/nbt1029PMID 15529165
• 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.

• Identification of a redox‐regulated chaperone network

  2004cited by this paper
• The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures.

  2004cited by this paper
• ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes.

  2004cited by this paper
• Substrate recognition by the AAA+ chaperone ClpB

  2004cited by this paper
• Phage Shock Protein PspA of Escherichia coli Relieves Saturation of Protein Export via the Tat Pathway

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• Cold-shock induced high-yield protein production in Escherichia coli

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• Successive and Synergistic Action of the Hsp70 and Hsp100 Chaperones in Protein Disaggregation*

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• A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function

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• Protein expression technologies: current status and future trends

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• Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.

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• A New Strategy for the Synthesis of Glycoproteins

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• Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.

  2004cited by this paper
• FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli.

  2004cited by this paper
• Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.

  2004cited by this paper
• Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed.

  2004cited by this paper
• Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway

  2003cited by this paper
• OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain.

  2003cited by this paper
• An alternative model of the twin arginine translocation system.

  2003cited by this paper
• The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

  2003cited by this paper
• The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state.

  2003cited by this paper
• The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins*

  2003cited by this paper
• Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

  2003cited by this paper
• Disulfide bond isomerization in prokaryotes.

  2003cited by this paper
• Protein disulfide bond formation in prokaryotes.

  2003cited by this paper
• Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX.

  2003cited by this paper
• Moving folded proteins across the bacterial cell membrane.

  2003cited by this paper
• Improving heterologous protein folding via molecular chaperone and foldase co-expression.

  2003cited by this paper
• Practical considerations in refolding proteins from inclusion bodies.

  2003cited by this paper
• Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase.

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• Join the crowd

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• Trigger Factor and DnaK possess overlapping substrate pools and binding specificities

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• Protein unfolding--an important process in vivo?

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• Role of molecular chaperones in inclusion body formation

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• Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli

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• The bacterial translocase: a dynamic protein channel complex

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• Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK‐DnaJ‐GrpE system in the management of protein misfolding under severe stress conditions

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• Characterization of the Escherichia coli YedU protein as a molecular chaperone.

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• Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli.

  2002cited by this paper
• Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

  2002cited by this paper
• Trigger Factor Retards Protein Export in Escherichia coli*

  2002cited by this paper
• Escherichia coli DegP Protease Cleaves between Paired Hydrophobic Residues in a Natural Substrate: the PapA Pilin

  2002cited by this paper
• Directed evolution of substrate-optimized GroEL/S chaperonins.

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• Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

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• Redox-regulated molecular chaperones

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• α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network

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• PDZ Domains Facilitate Binding of High Temperature Requirement Protease A (HtrA) and Tail-specific Protease (Tsp) to Heterologous Substrates through Recognition of the Small Stable RNA A (ssrA)-encoded Peptide*

  2002cited by this paper
• Genetic Analysis of the Twin Arginine Translocator Secretion Pathway in Bacteria*

  2002cited by this paper
• N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

  2002cited by this paper
• Long-term and homogeneous regulation of the Escherichia coli araBAD promoter by use of a lactose transporter of relaxed specificity

  2002cited by this paper
• ClpS, a substrate modulator of the ClpAP machine.

  2002cited by this paper
• Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.

  2002cited by this paper
• Hsp31, the Escherichia coli yedU Gene Product, Is a Molecular Chaperone Whose Activity Is Inhibited by ATP at High Temperatures*

  2002cited by this paper
• Overproduction of Bacterial Protein Disulfide Isomerase (DsbC) and Its Modulator (DsbD) Markedly Enhances Periplasmic Production of Human Nerve Growth Factor in Escherichia coli *

  2001cited by this paper
• Current Status and Future Trends

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• Roles of thiol-redox pathways in bacteria.

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• The structural basis of protein targeting and translocation in bacteria

  2001cited by this paper
• The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

  2001cited by this paper
• Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli

  2001cited by this paper
• Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase

  2001cited by this paper
• Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site

  2001cited by this paper
• Molecular chaperones in the cell

  2001cited by this paper
• Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

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• Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones.

  2001cited by this paper
• A Pair of Fluorescent Resonance Energy Transfer-based Probes for Tyrosine Phosphorylation of the CrkII Adaptor Protein in Vivo * 210

  2001cited by this paper
• Homogeneous expression of the P(BAD) promoter in Escherichia coli by constitutive expression of the low-affinity high-capacity AraE transporter.

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• Binding specificity of Escherichia coli trigger factor

  2001cited by this paper
• Kinetics of Heat‐Shock Response and Inclusion Body Formation During Temperature‐Induced Production of Basic Fibroblast Growth Factor in High‐Cell‐Density Cultures of Recombinant Escherichiacoli

  2000cited by this paper
• Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli

  2000cited by this paper
• The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA

  2000cited by this paper
• The structures of HsIU and the ATP-dependent protease HsIU-HsIV.

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• Secretory production of human leptin in Escherichia coli.

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• Overexpression of Protein Disulfide Isomerase DsbC Stabilizes Multiple-Disulfide-Bonded Recombinant Protein Produced and Transported to the Periplasm in Escherichia coli

  2000cited by this paper
• Crystal structure of the bacterial protein export chaperone SecB

  2000cited by this paper
• Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery*

  2000cited by this paper
• The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA

  2000cited by this paper
• The structures of HslU and the ATP-dependent protease HslU–HslV

  2000cited by this paper
• Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli

  2000cited by this paper
• Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

  1999cited by this paper
• Skp, a Molecular Chaperone of Gram-negative Bacteria, Is Required for the Formation of Soluble Periplasmic Intermediates of Outer Membrane Proteins*

  1999cited by this paper
• Biochemical Characterization of the Small Heat Shock Protein IbpB from Escherichia coli*

  1999cited by this paper
• ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein Aggregation

  1999cited by this paper
• Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

  1999cited by this paper
• Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments.

  1999cited by this paper
• Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli: application to the production of a toxic and proteolytically sensitive fusion protein.

  1999cited by this paper
• A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

  1999cited by this paper
• The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network*

  1998cited by this paper
• PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA–SecY interaction during the initiation of translocation

  1998cited by this paper
• Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins

  1998cited by this paper
• The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system.

  1998cited by this paper
• Chaperone Coexpression Plasmids: Differential and Synergistic Roles of DnaK-DnaJ-GrpE and GroEL-GroES in Assisting Folding of an Allergen of Japanese Cedar Pollen, Cryj2, inEscherichia coli

  1998cited by this paper
• Overlapping functions of components of a bacterial Sec‐independent protein export pathway

  1998cited by this paper
• Expression of Active Human Tissue-Type Plasminogen Activator in Escherichia coli

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• Scale‐up and Optimization of the Low‐Temperature Inducible cspA Promoter System

  1998cited by this paper
• Selection for a periplasmic factor improving phage display and functional periplasmic expression

  1998cited by this paper
• Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria.

  1998cited by this paper
• TolAIII co-overexpression facilitates the recovery of periplasmic recombinant proteins into the growth medium of Escherichia coli.

  1998cited by this paper
• The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasm*

  1997cited by this paper
• Efficient production of heat-labile enterotoxin mutant proteins by overexpression of dsbA in a degP-deficient Escherichia coli strain

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• In vivo observation of polypeptide flux through the bacterial chaperonin system.

  1997cited by this paper
• Expression of aggregation-prone recombinant proteins at low temperatures: a comparative study of the Escherichia coli cspA and tac promoter systems.

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