DnaK from Vibrio proteolyticus : Complementation of a dnaK-Null Mutant of Escherichia coli and the Role of Its ATPase Domain (Enzymology, Protein Engineering, and Enzyme Technology)
スポンサーリンク
概要
- 論文の詳細を見る
We cloned the 4.8-kbp DNA fragment containing the dnaK gene from the chromosomal DNA of Vibrio proteolyticus. It contained four genes arranged unidirectionally in the order of grpE, gltP, dnaK and dnaJ. The DnaK gene of V. proteolyticus (VprDnaK) allowed a dnaK-null mutant of Escherichia coli (ΔdnaK52) to propagateλphages but not to grow at 43℃. However, a chimeric DnaK gene comprising the regions corresponding to the N-terminal ATPase domain of E. coli DnaK (EcoDnaK) and the C-terminal region of VprDnaK including the substrate-binding domain, enabled the mutant to grow at 43℃. The temperature dependence for the ATPase activity of the chimeric DnaK was similar to that of EcoDnaK. Fluorometric analyses showed that the chimeric DnaK is much more thermostable than EcoDnaK and VprDnaK. These findings indicate that the thermal stability of the ATPase domain of DnaK is responsible for its chaperone action at high temperatures such as 43℃.
- 社団法人日本生物工学会の論文
- 2005-02-25
著者
-
Esaki N
Institute For Chemical Research Kyoto University
-
Esaki Nobuyoshi
Kyoto Univ.
-
Esaki Nobuyoshi
Nstitute For Chemical Research Kyoto University
-
Esaki Nobuyoshi
京都大学化学研究所 分子微生物科学
-
Ezaki Nobuyoshi
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
-
Esaki Nobuyoshi
Institute for Chemical Research, Kyoto University
-
YOSHIMURA Tohru
Institute for Chemical Research, Kyoto University
-
Esaki Nobuyoshi
Inst. For Chemical Res. Kyoto Univ.
-
GALKIN Andrey
Institute for Chemical Resarch, Kyoto University
-
YOSHIMUNE KAZUAKI
Institute for Chemical Research, Kyoto University
-
KULAKOVA LJUDMILA
Institute for Chemical Research, Kyoto University
-
Esaki N
Kyoto Univ.
-
Yoshimura Tohru
Institute For Chemical Research Kyoto University:(present Address)department Of Applied Molecular Bi
-
Esaki Nobuyoshi
Kyoto Univ. Kyoto Jpn
-
Esaki Nobuyoshi
Institute For Chemical Resarch Kyoto University
-
Kulakova Ljudmila
Institute For Chemical Research Kyoto University
-
Galkin A
Institute For Chemical Research Kyoto University
-
Yoshimune Kazuaki
Institute For Chemical Research Kyoto University:(present Address)department Of Applied Chemistry Fa
関連論文
- Production of (S)-2-Chloropropionate by Asymmetric Reduction of 2-Chloroacrylate with 2-Haloacrylate Reductase Coupled with Glucose Dehydrogenase(BIOCHEMICAL ENGINEERING)
- Serine Racemase with Catalytically Active Lysinoalanyl Residue
- Amino Acid Racemases : Functions and Mechanisms
- Gene Cloning, Purification, and Characterization of 2, 3-Diaminopropionate Ammonia-lyase from Escherichia coli(Biochemistry & Molecular Biology)
- Stereospecificity for the Hydrogen Transfer of Pyridoxal Enzyme Reactions
- Gene Cloning, Purification, and Characterization of Two Cyanobacterial NifS Homologs Driving Iron-Sulfur Cluster Formation
- Stereochemistry of the Transamination Reaction Catalyzed by Aminodeoxychorismate Lyase from Escherichia coli: Close Relationship between Fold Type and Stereochemistry
- Three-Dimensional Structure of 4-Amino-4-Deoxychorismate Lyase from Escherichia coli
- Kinetic and Mutational Studies of Three NifS Homologs from Esherichia coli: Mechanistic Difference between L-Cysteine Desulfurase and L-Selenocysteine Lyase Reactions
- A Novel Zinc-containing α-Keto Ester Reductase from Actinomycete : An Approach Based on Protein Chemistry and Bioinformatics
- Mechanism of Inactivation of α-Amino-ε-caprolactam Racemase by α-Amino-δ -valerolactam
- Synthesis of Selenocystine and Selenohomocystine with O-Acetylhomoserine Sulfhydrylase
- Cloning and Expression of the Pseudomonas Gene for Utilization of D-Leucine in Escherichia coli
- Action of S-Carbamoyl and S-Thiocarbamoyl Derivatives of L-Cysteine on L-Amino Acid Oxidase
- Inactivation of Amino Acid Racemase by S-(N-Methylthiocarbamoyl)- D, L-cysteine
- Reactions of O-Substituted L-Homoserines Catalyzed by L-Methionine y-Lyase and Their Mechanism
- Purification and Properties of L-Methionine γ-Lyase from Aeromonas sp.
- Enzymatic Synthesis of S-Substituted L-Cysteines with Tryptophan Synthase of Escherichia coli
- Properties of α-Amino-ε-caprolactam Racemasefrom Achromobacter obae
- Catalysis-Linked Inactivation of Fluoroacetate Dehalogenase by Ammonia: A Novel Approach to Probe the Active-Site Environment
- X-Ray Structure of a Reaction Intermediate of L-2-Haloacid Dehalogenase with L-2-Chloropropionamid
- Primary Structure and Catalytic Properties of a Cold-active Esterase from a Psychrotroph, Acinetobacter sp. Strain No.6. Isolated from Siberian Soil(Biochemistry & Molecular Biology)
- Cold-Active Lipolytic Activity of Psychrotrophic Acinetobacter sp. Strain No.6
- Production of New Tricarboxylic Acid Anhydrides from Stearic Acid by Pseudomonas cepacia A-1419
- Biotransformation of Oleic Acid by Alcaligenes sp. 5-18,a Bacterium Tolerant to High Concentrations of Oleic Acid
- Biotransformation of Oleic Acid by Micrococcus luteus Cells
- Transformation of Oleic Acid and Its Esters by Sarcina lutea(Microbiology & Fermentation Industry)
- Identification of Proteins Interacting with Selenocysteine Lyase
- Thioredoxin Reductase 1 Is Important for Selenoprotein Biosynthesis in HeLa Cells
- Enzymatic Synthesis of L-Pipecolic Acid by Δ^1-Piperideine-2-carboxylate Reductase from Pseudomonas putida
- Selenoprotein Biosynthesis and Selenium-Specific Enzymes (特集1:若手が拓く微量元素研究の最前線)
- Protein Interaction between Selenophosphate Synthetase and IscS
- RNAi-mediated knock down of mammalian selenocysteine lyase
- A New Family of NAD(P)H-Dependent Oxidoreductases Distinct from Conventional Rossmann-Fold Proteins
- Network of Protein-Protein Interactions among Iron-Sulfur Cluster Assembly Proteins in Escherichia coli
- Structure of External Aldimine of Escherichia coli CsdB, an IscS/NifS Homolog: Implications for Its Specificity toward Selenocysteine
- Tyrosine 265 of Alanine Racemase Serves as a Base Abstracting α-Hydrogen from L-Alanine: The Counterpart Residue to Lysine 39 Specific to D-Alanine
- 2-Haloacrylate hydratase is a bifunctional enzyme with NADH-dependent FAD reductase activity
- Comprehensive Site-Directed Mutagenesis of L-2-Halo Acid Dehalogenase to Probe Catalytic Amino Acid Residues
- Two Kinds of 2-Halo Acid Dehalogenases from Pseudomonas sp. YL Induced by 2-Chloroacrylate and 2-Chloropropionate
- Role of Tyrosine 265 of Alanine Racemase from Bacillus stearothermophilus
- The Distribution of Phosphatidyl-D-serine in the Rat
- Primary Structure and Properties of Bacterial Formate Dehydrogenase From Moraxella sp C-1
- Thermostable Ornithine Aminotransferase from Bacillus sp. YM- 2: Purification and Characterization
- Structural Analysis of the L-Methionine γ-Lyase Gene from Pseudomonas putida^1
- Role of Leucine 201 of Thermostable D-Amino Acid Aminotransferase from a Thermophile, Bacillus sp. YM-1
- In Vivo Effect of GroESL on the Folding of Glutamate Racemase of Escherichia coli
- 364 Thermostable Formate Dehydrogenase from Mycobacterium vaccae N10; Structure and Function
- Large-Scale Production of Thermostable Alanine Dehydrogenase from Recombinant Cells
- Total Conversion of Racemic 2-Chloropropionic Acid into D-Lactate by Combination of Enzymatic and Chemical Dehalogenations
- 411 Enzymatic Dehalogenation of 2-Halo Acids in Nonaqueous Medium
- Characterization of Human Selenocysteine Synthase Involved in Selenoprotein Biosynthesis
- Functional Analysis of Two Homologous Mouse Selenophosphate Synthetases
- DnaK from Vibrio proteolyticus : Complementation of a dnaK-Null Mutant of Escherichia coli and the Role of Its ATPase Domain (Enzymology, Protein Engineering, and Enzyme Technology)
- Kinetics of Thermostable Alanine Racemase of Bacillus stearothermophilus
- Lysyl-tRNA Synthetase of Bacillus stearothermophilus Molecular Cloning and Expression of the Gene
- Crystal Structure of the Pyridoxal 5'-phosphate Dependent L-Methionine γ-Lyase from Pseudomonas putida
- Structure of the Antitumour Enzyme L-Methionine γ-Lyase from Pseudomonas putida at 1.8A Resolution
- Role of Tyrosine 114 of L-Methionine γ-lyase from Pseudomonas putida
- Transamination as a Side-Reaction catalyzed by Alanine Racemase of Bacillus stearothermophilus
- Construction and Properties of a Fragmentary D-Amino Acid Aminotransferase
- Stereospecific Labeling at α-Position of Phenylalanine and Phenylglycine with Amino Acid Racemase
- Compensation for D-Glutamate Auxotrophy of Escherichia coli WM335 by D-Amino Acid Aminotransferase Gene and Regulation of murI Expression
- Mutation of Arginine 98, Which Serves as a Substrate-Recognition Site of D-Amino Acid Aminotransferase, Can Be Partly Compensated for by Mutation of Tyrosine 88 to an Arginyl Residue
- Cloning and Expression of the Glutamate Racemase Gene of Bacillus pumilus^1
- Conversion of α-Keto Acids to D-Amino Acids by Coupling of Four Enzyme Reactions
- Glutamate Racemase of E. coli : Recharacterization of the Activation by UDP-N -Acetylmuramoyl-L-Alanine
- Reconstitution of Fragmentary Form of Thermostable Alanine Racemase
- A Novel NADH-Dependent Carbonyl Reductase from Kluyveromyces aestuarii and Comparison of NADH-Regeneration System for the Synthesis of Ethyl (S)-4-Chloro-3-hydroxybutanoate
- Catalytic Action of L-Methionine γ-Lyase on 4-Azaleucine(Biological Chemistry)
- Chemical Modification of Cysteine Residues of _L-Methionine γ-Lyase(Biological Chemistry)
- Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum
- Effects of Pyridoxal 5'-Phosphate on the Refolding of Aspartate Aminotransferase
- Limited Proteolysis of Thermostable Alanine Racemase of Bacillus stearothremophilus(Biological Chemistry)
- Stereospeciticity for the Hydrogen Transfer and Molecular Evolution of Pyridoxal Enzymes
- Inactivation of Glutamate Racemase of Pediococcus pentosaceus with L-Serine O-Sulfate
- Thermolabile Alanine Racemase from a Psychrotroph, Pseudomonas fluorescens : Purification and Properties
- Total Conversion of Racemic Pipecolic Acid into the L-Enantiomer by a Combination of Enantiospecific Oxidation with D-Amino Acid Oxidase and Reduction with Sodium Borohydride
- Synthesis of L-Proline form the Racemate by Coupling of Enzymatic Enantiospecific Oxidation and Chemical Non-Enantiospecific Reduction
- Decomposition of L-Selenodjenkolate Catalyzed by S-Alkylcysteine α,β-Lyase(Biological Chemistry)
- Continuous Conversion to Optically Pure L-Methionine from D-Enantiomer Contaminated Preparations by an Immobilized Enzyme Membrane Reactor
- Thermostable S-Alkylcysteine α,β-Lyase from a Thermophile : Purification and Properties(Biological Chemistry)
- Selenite Assimilation into Formate Dehydrogenase H Depends on Thioredoxin Reductase in Escherichia coli
- Gene Clonign, Purification, and Characterization of the Highly Thermostable Leucine Dehydrogenase of Bacillus sp.
- Gene Cloning, Purification and Characterization of Thermostable Alanine Dehydrogenase of Bacillus stearothermophilus
- Leucine Dehydrogenase of an Thermophilic Anaerobe, Clostridium thermoaceticum: Gene Cloning, Purification and Characterization(Microbiology & Fermentation Industry)
- The Role of Cysteine 116 in the Active Site of the Antitumor Enzyme L-Methionine γ-Lyase from Pseudomonas putida
- The Role of Cysteine 116 in the Active Site of the Antitumor Enzyme L-Methionine γ-Lyase from Pseudomonas putida
- The Distribution of Phosphatidyl-D-serine in the Rat
- Selenocysteine Is Selectively Taken Up by Red Blood Cells
- Identification of Proteins Interacting with Selenocysteine Lyase
- Expression analysis of mammalian selenocysteine lyase
- Determination by ^1H-NMR of the Stereospecificity of NAD-dependent Plant L-Histidinol Dehydrogenase for Nicotinamide C-4 Hydrogen Transfer
- Effects of Selenium Deficiency on the Expression of Selenoprotein mRNAs in Mouse Brain
- Specific transfer of selenium in selenoprotein biosynthesis
- Role of Cysteine Desulfurase in the Biosynthesis of Formate Dehydrogenase H Containing Mo, Molybdopterin, Selenocysteine, and Fe_4S_4 Cluster
- Protein Interaction between Selenocysteine Lyase and MUP-I
- The C_3-N Bond Cleavage of 2-Amino-3-(N-substituted-amino)-propionic Acids Catalyzed by L-Methionine γ-Lyase(Biological Chemistry)
- Mammalian Selenocysteine Lyase Is Involved in Selenoprotein Biosynthesis
- Selenite Reduction by the Thioredoxin System : Kinetics and Identification of Protein-Bound Selenide