T4
|
DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase.
|
kcat
|
145 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (with heparin); Experimental conditions: Temp (37°C), Mg++ (8mM)
|
T4
|
DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase.
|
kcat
|
106 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Multiple Turnover (without heparin); Experimental conditions: Mg++ (8mM), Temp (37°C)
|
T4
|
Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities.
|
Processivity
|
12bp
|
|
T4
|
Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities.
|
KM
|
2uM
|
Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
|
T4
|
Fidelity of DNA polymerases in DNA amplification.
|
Nucleotide Substitution Rate
|
3E-06 errors/bp
|
Technique: DGGE
|
T4
|
On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro.
|
Nucleotide Substitution Rate
|
1E-06 errors/bp
|
Technique: Reversion (1 mM dNTP)
|
T4
|
On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro.
|
Processivity
|
1840bp
|
|
T4
|
Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase.
|
Nucleotide Substitution Rate
|
1E-06 errors/bp
|
Technique: Gel kinetic assay (dCMP-A mismatch)
|
T4
|
Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase.
|
Nucleotide Substitution Rate
|
1E-05 errors/bp
|
Technique: Gel kinetic assay (dGMP-A mismatch)
|
T4
|
Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase.
|
Nucleotide Substitution Rate
|
1E-08 errors/bp
|
Technique: Gel kinetic assay (dAMP-A mismatch)
|
T4
|
Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase.
|
Nucleotide Substitution Rate
|
0.0002 errors/bp
|
Technique: Gel kinetic assay (dTMP-T mismatch)
|
T4
|
Stopped-flow fluorescence study of precatalytic primer strand base-unstacking transitions in the exonuclease cleft of bacteriophage T4 DNA polymerase.
|
Methods Featured
|
Fluorescence Spectroscopy
|
|
T4
|
Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms.
|
KM
|
4.6uM
|
Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Primer extension assay
|
T4
|
Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms.
|
KM
|
25.9uM
|
Reaction: Nucleotide incorporation; Substrate: n/a; Technique: Primer extension assay (2AP)
|
T4
|
Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system.
|
Vmax
|
500 /second
|
Reaction: Nucleotide incorporation; Substrate: dNTPs
|
T4
|
Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system.
|
Nucleotide incorporation accessory protein(s)
|
gp 32, gp 45, gp 44/62, gp 41
|
|
T4
|
The 3'-5' proofreading exonuclease of bacteriophage T4 DNA polymerase is stimulated by other T4 DNA replication proteins.
|
Exonuclease accessory protein(s)
|
gp 45, gp 44/62, gp 32
|
|
T4
|
Using 2-aminopurine fluorescence to detect bacteriophage T4 DNA polymerase-DNA complexes that are important for primer extension and proofreading reactions.
|
Methods Featured
|
Fluorescence Spectroscopy
|
|
T4
|
Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase.
|
kcat
|
200 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Degradation of labeled single-stranded DNA
|
T4
|
Exonuclease-polymerase active site partitioning of primer-template DNA strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA polymerase.
|
Methods Featured
|
Fluorescence Spectroscopy
|
|
T4
|
Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22.
|
KM
|
0.04uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22.
|
KM
|
0.08uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22.
|
Vmax
|
91 /minute
|
Reaction: 3-5' Exonuclease
|
T4
|
Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22.
|
Vmax
|
2.2 /minute
|
Reaction: 3-5' Exonuclease; Technique: Steady State (substrate: E. coli DNA, heat denatured)
|
T4
|
Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69.
|
Kd
|
43nM
|
Reaction: Polymerase-DNA interaction; Substrate: DNA template
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
Molecular Weight
|
1.15E+05 Dalton
|
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
Cloned or native
|
Native organism
|
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
Tagged
|
No
|
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
Full length or truncated
|
Full length
|
|
T4
|
On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase.
|
Specific Activity
|
2.3E+04 units/mg
|
|
T4
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity.
|
KM
|
1000uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity.
|
KM
|
7uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity.
|
kcat
|
170 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity.
|
kcat
|
420 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase.
|
KM
|
6.9uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase.
|
KM
|
0.4uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase.
|
kcat
|
65.1 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase.
|
kcat
|
0.16 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases.
|
Vmax
|
1100 /minute
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (37°C)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases.
|
Vmax
|
350 /minute
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (37°C)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases.
|
Vmax
|
850 /minute
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (30°C)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases.
|
Vmax
|
27 /minute
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (30°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
KM
|
17uM
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
KM
|
17uM
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
KM
|
47uM
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (30°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
Vmax
|
0.33 /minute
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
Vmax
|
0.66 /minute
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
|
T4
|
An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme.
|
Vmax
|
0.15 /minute
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
1600uM
|
Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
1.9uM
|
Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
17uM
|
Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
1.3uM
|
Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
6uM
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
1.8uM
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
190uM
|
Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
KM
|
1.3uM
|
Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
60 /minute
|
Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
60 /minute
|
Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
800 /minute
|
Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
1120 /minute
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
80 /minute
|
Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
160 /minute
|
Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
50 /minute
|
Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template.
|
Vmax
|
54 /minute
|
Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
12.3uM
|
Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Template: poly (dG)-(dC))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
38uM
|
Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (Template: poly(dA)-(dT))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
605uM
|
Reaction: Misincorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dA)-(dT))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
5950uM
|
Reaction: Misincorporation; Substrate: dCTP; Technique: Steady State (Template: poly(dA)-(dT))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
1850uM
|
Reaction: Misincorporation; Substrate: dATP; Technique: Steady State (Template: poly(dG)-(dC))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
4940uM
|
Reaction: Misincorporation; Substrate: dTTP; Technique: Steady State (Template: poly(dG)-(dC))
|
T4
|
Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro.
|
KM
|
6.4uM
|
Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dG)-(dC))
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
Incorporation of non-standard nucleotides
|
Unspecified
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
Cloned or native
|
Unspecified
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
5-3' Exonuclease
|
Unspecified
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
Tagged
|
Unspecified
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
Full length or truncated
|
Unspecified
|
|
T4
|
Incorporation of reporter-labeled nucleotides by DNA polymerases.
|
Application name
|
PCR
|
|
T4
|
On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation.
|
Cloned or native
|
Native organism
|
|
T4
|
On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation.
|
Tagged
|
No
|
|
T4
|
On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation.
|
Full length or truncated
|
Full length
|
|
T4
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
|
kcat
|
130 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
|
T4
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
|
kcat
|
91 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template
|
T4
|
Characterization of the stimulatory effect of T4 gene 45 protein and the gene 44/62 protein complex on DNA synthesis by T4 DNA polymerase.
|
Processivity
|
3000bp
|
|
T4
|
Characterization of the stimulatory effect of T4 gene 45 protein and the gene 44/62 protein complex on DNA synthesis by T4 DNA polymerase.
|
Nucleotide incorporation accessory protein(s)
|
44/62 and 45 proteins
|
|
T4
|
A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease.
|
Cloned or native
|
Cloned in E. coli
|
|
T4
|
A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease.
|
Full length or truncated
|
Full length
|
|
T4
|
A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease.
|
Specific Activity
|
3039 units/mg
|
|
T4
|
Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork.
|
Full length or truncated
|
Full length
|
|
T4
|
Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork.
|
Processivity
|
380bp
|
|
T4
|
Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork.
|
Vmax
|
400 /second
|
Reaction: Nucleotide incorporation; Substrate: dNTPs
|
T4
|
Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis.
|
Cloned or native
|
Cloned in E. coli
|
|
T4
|
Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis.
|
Full length or truncated
|
Full length
|
|
T4
|
Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis.
|
Processivity
|
1500bp
|
|
T4
|
The dynamic processivity of the T4 DNA polymerase during replication.
|
Full length or truncated
|
Full length
|
|
T4
|
The dynamic processivity of the T4 DNA polymerase during replication.
|
Vmax
|
150 /second
|
Reaction: Nucleotide incorporation; Substrate: dNTPs
|
T4
|
The dynamic processivity of the T4 DNA polymerase during replication.
|
Kd
|
145nM
|
Reaction: Nucleotide incorporation; Substrate: dNTPs
|
T4
|
The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme.
|
3-5' Exonuclease (proofreading)
|
Unspecified
|
|
T4
|
The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme.
|
Cloned or native
|
Cloned in E. coli
|
|
T4
|
The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme.
|
5-3' Exonuclease
|
Unspecified
|
|
T4
|
The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme.
|
Full length or truncated
|
Full length
|
|
T4
|
The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme.
|
Processivity
|
46bp
|
|
T4
|
RNA priming of DNA replication by bacteriophage T4 proteins.
|
Extension from RNA primer
|
Yes
|
|
T4
|
Pentaribonucleotides of mixed sequence are synthesized and efficiently prime de novo DNA chain starts in the T4 bacteriophage DNA replication system.
|
Extension from RNA primer
|
Yes
|
|
T4
|
Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis.
|
Extension from RNA primer
|
Yes
|
|
T4
|
Bacteriophage T4 DNA primase-helicase. Characterization of the DNA synthesis primed by T4 61 protein in the absence of T4 41 protein.
|
Extension from RNA primer
|
Yes
|
|
T4
|
DNA synthesis on a double-stranded DNA template by the T4 bacteriophage DNA polymerase and the T4 gene 32 DNA unwinding protein.
|
Nick Extension
|
Yes, unspecified mechanism
|
|
T4
|
Bacteriophage T4 RNase H removes both RNA primers and adjacent DNA from the 5' end of lagging strand fragments.
|
RNase H
|
Yes
|
|
T4
|
The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis.
|
5-3' Exonuclease
|
No
|
|
T4
|
The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis.
|
Extension from RNA primer
|
Yes
|
|
T4
|
Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers.
|
5-3' Exonuclease
|
No
|
|
T4
|
Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers.
|
Extension from RNA primer
|
Yes
|
|
T4
|
Spectrum of spontaneous frameshift mutations. Sequences of bacteriophage T4 rII gene frameshifts.
|
Frameshift Error Rate
|
3E-07 errors/bp
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Molecular Weight
|
1.12E+05 Dalton
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
5-3' Exonuclease
|
No
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Full length or truncated
|
Full length
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Optimal pH
|
pH 8.5
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Specific Activity
|
3.3E+04 units/mg
|
Technique: Polymerase Assay (calf thymus DNA)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Strand Displacement
|
No
|
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
0 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Mg++ (6mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
75 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Mg++ (.1mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
0 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: NTPs (0mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
49 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0mM), CTP (0mM), TTP (0mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
81 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0.2mM), CTP (0mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Percent/Fold Effect
|
96 % decrease
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0.2mM), CTP (0.2mM), TTP (0mM)
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4.
|
Gap Filling
|
Yes
|
|
T4
|
Effect of accessory proteins on T4 DNA polymerase replication fidelity.
|
3-5' Exonuclease (proofreading)
|
Yes
|
|
T4
|
Effect of accessory proteins on T4 DNA polymerase replication fidelity.
|
5-3' Exonuclease
|
Unspecified
|
|
T4
|
Effect of accessory proteins on T4 DNA polymerase replication fidelity.
|
Frameshift Error Rate
|
1.2E-06 errors/bp
|
Technique: M13mp2 forward mutation assay
|
T4
|
Effect of accessory proteins on T4 DNA polymerase replication fidelity.
|
Nucleotide Substitution Rate
|
9.4E-07 errors/bp
|
Technique: M13mp2 forward mutation assay
|
T4
|
Effect of accessory proteins on T4 DNA polymerase replication fidelity.
|
Nucleotide Substitution Rate
|
3.3E-06 errors/bp
|
Technique: M13mp2 opal codon reversion assay
|
T4
|
Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break.
|
5-3' Exonuclease
|
No
|
|
T4
|
A constant rate of spontaneous mutation in DNA-based microbes.
|
Overall Error Rate
|
2E-08 errors/bp
|
Technique: rII+ reversion
|