The Chemical Chaperone Proline Relieves the Thermosensitivity of a dnaK Deletion Mutant at 42°C (original) (raw)

The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42 degrees C

Journal of bacteriology, 2004

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

Axel Mogk, Toshifumi Tomoyasu

Molecular Microbiology, 2001

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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB

Axel Mogk, Toshifumi Tomoyasu

The EMBO Journal, 1999

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Dicarboxylic amino acids and glycine-betaine regulate chaperone-mediated protein-disaggregation under stress

Anat Ben-zvi, David Rosenthal

Molecular Microbiology, 2003

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Chaperone-Facilitated Aggregation of Thermo-Sensitive Proteins Shields Them from Degradation during Heat Stress

Luis Marte

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Heterologous expression of an engineered protein domain acts as chaperone and enhances thermotolerance of Escherichia coli

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Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase

Wilbert Boelens

Extremophiles, 2007

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Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology

Axel Mogk

Journal of Biotechnology, 2002

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Stabilized homoserine o-succinyltransferases (MetA) or L-methionine partially recovers the growth defect in Escherichia coli lacking ATP-dependent proteases or the DnaK chaperone

Elena Mordukhova

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Mantu Santra

Proceedings of the National Academy of Sciences of the United States of America, 2017

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DnaK functions as a central hub in the E. coli chaperone network

Manajit Hayer-Hartl

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The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli

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Temperature-dependent proteolysis as a control element in Escherichia coli metabolism

Chen Katz

Research in Microbiology, 2009

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Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism

Mickael Dinclaux

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The Influence of Chemical Chaperones on Enzymatic Activity under Thermal and Chemical Stresses: Common Features and Variation among Diverse Chemical Families

Guy Shmul

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Theoretical and experimental investigation of chaperone effects on soluble recombinant proteins in Escherichia coli: effect of free DnaK level on temperature-induced recombinant streptokinase production

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Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

Alexander Gragerov

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Role of the Heat-Shock Response in the Life and Death of Proteins

R. Morimoto

Annals of the New York Academy of Sciences, 1998

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Site-directed mutagenesis of the HtrA(DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures

Joanna Skórko-glonek

Gene, 1995

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Defense against Protein Carbonylation by DnaK/DnaJ and Proteases of the Heat Shock Regulon

Manuel Ballesteros

Journal of Bacteriology, 2005

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Satyam Tiwari

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Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli

Lila Gierasch

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Igor Berezovsky

Wiley Encyclopedia of Chemical Biology, 2007

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Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli

F. Schwager

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Sandeep Sharma

2011

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Comprehensive Analysis of Protein Folding Activation Thermodynamics Reveals a Universal Behavior Violated by Kinetically Stable Proteases

Ken Dill

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The 70-kDa Heat-Shock Protein/DnaK Chaperone System is Required for the Productive Folding of Ribulose-Bisphosphate Carboxylase Subunits in Escherichia Coli

Susana Checa

European Journal of Biochemistry, 1997

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Enhancement of the Chaperone Activity of AhpC from Pseudomonas aeruginosa PAO1 Resulting from a Point-specific Mutation Confers Heat Tolerance in Escherichia coli

Bhumi Nath Tripathi

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Successive action of Escherichia coli chaperones in vivo

Alexander Gragerov

Molecular Microbiology, 1994

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Mutual Interaction Study Between DnaK-GroEL-FtSH with Heat Shock Regulator σ32 to Explain Prokaryotic Heat Shock Regulation

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The Chemical Chaperone Proline Relieves the Thermosensitivity of a dnaK Deletion Mutant at 42°C (original) (raw)

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