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ATP + ATP
A(pA)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dT)30 supports extensive DNA and RNA synthesis. Oligo(dT)30 supports the synthesis of shorter RNA chains than those formed in the presence of oligo(dC)30 as well as the production of higher levels of RNA than DNA
-
-
?
ATP + n ATP
A(pA)n + n diphosphate
dATP + dATP
dA(pdA)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dT)30 supports extensive DNA and RNA synthesis
-
-
?
dATP + glycerol
dAMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dATP + Tris
dAMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dCTP + glycerol
dAMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dCTP + Tris
dAMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dGTP + glycerol
dGMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dGTP + n dGTP
dG(pdG)n + n diphosphate
dGTP + Tris
dGMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
dNTP + n NTP
(dNTP)n+1 + n diphosphate
Q9V292; Q9V291
DNA primase has comparable affinities for ribonucleotides and deoxyribonucleotides. The Pabp41 subunit alone has no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. DNA primase also displayed DNA polymerase, gapfilling, and strand-displacement activities
-
-
?
dTTP + glycerol
dTMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dTTP + Tris
dTMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
NTP + n NTP
N(pN)n + n diphosphate
additional information
?
-
ATP + n ATP
A(pA)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
ATP + n ATP
A(pA)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dGTP + n dGTP
dG(pdG)n + n diphosphate
the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation
-
-
?
dGTP + n dGTP
dG(pdG)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dC)30 supports extensive DNA and RNA synthesis. Of the four homo-oligodeoxynucleotides, 30 nt in length oligo(dC)30 is the most effective template supporting extensive DNA synthesis with dGTP. dGTP incorporation exceeds the level of oligo(dC)30 template added, and the lengths of DNA chains are 100 nt
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the p41-p46 primase preferentially uses dNTPs compared to NTPs. DNA strand synthesis is stimulated by the addition of NTPs or by addition of ATP to the same level. ATP is the preferable initiating nucleotide for the p41-p46 complex
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
de novo DNA synthesis is 10 times more effective than RNA synthesis
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(A)15/poly(dT) but with lower efficiency with respect to ATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(A)15/poly(dT) but with lower efficiency with respect to ATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
Q5JJ72; Q5JJ73
the enzyme supports both DNA and RNA synthesis, whereas the p41 subunit alone marginally produces RNA and synthesizes DNA chains that are longer than those formed by the complex. The primase complex preferentially interacts with dNTP rather than ribonucleoside triphosphates and initiates RNA as well as DNA chains de novo. The archaeal primase complex, in contrast to the eukaryote homolog, can initiate DNA chain synthesis in the absence of ribonucleoside triphosphates. DNA primers formed by the archaeal complex can be elongated extensively by the Thermococcus kodakaraensis DNA polymerase (Pol) B, whereas DNA primers formed by the p41 catalytic subunit alone are not
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dC)30 supports extensive DNA and RNA synthesis
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
synthesise oligoribonucleotides on various pyrimidine single-stranded DNA templates poly(dT) and poly(dC). The enzyme is almost completely inactive on a poly(dA) synthetic template
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
synthesise oligoribonucleotides on various pyrimidine single-stranded DNA templates poly(dT) and poly(dC). The enzyme is almost completely inactive on a poly(dA) synthetic template
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9V292; Q9V291
the multifunctional archaeal primase is involved in priming and repair
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9V292; Q9V291
DNA primase has comparable affinities for ribonucleotides and deoxyribonucleotides. The Pabp41 subunit alone has no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. DNA primase also displayed DNA polymerase, gapfilling, and strand-displacement activities
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the p41-p46 complex synthesizes the primers, which can be extended in the combination with other replication proteins from Pyrococcus furiosus
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the p41-p46 primase preferentially uses dNTPs compared to NTPs. The primase complex synthesizes RNA segments only when NTPs but not dNTPs are added as the substrates. When both dNTPs and NTPs exist at equal concentrations, no RNA products are observed. ATP is the preferable initiating nucleotide for the p41-p46 complex
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used as template with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. Products with an apparent length of 14 nt and 7 nt are mainly synthesised. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(rA)15/poly(dT) but with lower efficiency with respect to rATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used as template with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. Products with an apparent length of 14 nt and 7 nt are mainly synthesised. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(rA)15/poly(dT) but with lower efficiency with respect to rATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q5JJ72; Q5JJ73
the enzyme supports both DNA and RNA synthesis, whereas the p41 subunit alone marginally produces RNA and synthesizes DNA chains that are longer than those formed by the complex. The primase complex preferentially interacts with dNTP rather than ribonucleoside triphosphates and initiates RNA as well as DNA chains de novo. The archaeal primase complex, in contrast to the eukaryote homolog, can initiate DNA chain synthesis in the absence of ribonucleoside triphosphates. DNA primers formed by the archaeal complex can be elongated extensively by the Thermococcus kodakaraensis DNA polymerase (Pol) B, whereas DNA primers formed by the p41 catalytic subunit alone are not. When M13DNA is used as substrate all labeled rNTPs and dNTPs support RNA and DNA synthesis
-
-
?
additional information
?
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA. The site of interaction is mapped. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
-
?
additional information
?
-
usage of M13mp18ssDNA as a template
-
-
?
additional information
?
-
-
usage of M13mp18ssDNA as a template
-
-
?
additional information
?
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
primase PolpTN2 is able to prime the synthesis of dsDNA by Taq DNA polymerase and by DNA polymerase PolB encoded by the chromosome of Thermococcus nautili using M13mp18ssDNA as a template, method development and evaluation, overview. Mechanism of template-free synthesis of seeds by PolB and PolpTN2 from dNTP substrates
-
-
?
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K+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
Q9V292; Q9V291
optimal concentration: 10 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2
Mg2+
the enzyme is strictly dependent on divalent cations, activating metal preferably used by Rep245 for its DNA polymerase activity is Mg2+ at concentrations between 5 and 10 mM
Mn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mn2+
Q9V292; Q9V291
optimal concentration: 5 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2
Mn2+
the enzyme is strictly dependent on divalent cations, with Mn2+ as a cofactor, the DNA polymerase activity of Rep245 is optimal at 12.5 mM and decreases noticeably at increasing amounts of Mn2+
Mn2+
the enzyme requires manganese ions for catalytic activity
Mn2+
-
in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain
Mn2+
Q5JJ72; Q5JJ73
RNA synthesis with the Thermococcus kodakaraensis primase complex is stimulated about 2fold by the presence of Mn2+, whereas the size of RNA chains is marginally affected. DNA synthesis is slightly inhibited by Mn2+
Zn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Zn2+
the zinc ion is located within the loop region between beta-strand 6 and the prominent helix alpha4. It is coordinated by Cys 106 and His 108 of the loop and Cys114and Cys117 at the beginning of helix alpha4
Zn2+
contain one zinc ion in the small subunits. Residues Cys116, Cys119, Cys128 and Asp131 coordinate the zinc atom
additional information
Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245
additional information
-
Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245
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Adenocarcinoma
Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.
Adenocarcinoma
Incorporation of alpha-1-antichymotrypsin into human stomach adenocarcinoma cell nuclei and inhibition of DNA primase activity.
Breast Neoplasms
DNA primase polypeptide 1 (PRIM1) involves in estrogen-induced breast cancer formation through activation of the G2/M cell cycle checkpoint.
Carcinoma
Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.
Carcinoma
Incorporation of alpha-1-antichymotrypsin into human stomach adenocarcinoma cell nuclei and inhibition of DNA primase activity.
Carcinoma, Hepatocellular
DNA primase subunit 1 deteriorated progression of hepatocellular carcinoma by activating AKT/mTOR signaling and UBE2C-mediated P53 ubiquitination.
Carcinoma, Hepatocellular
DNA Primase Subunit 1 Expression in Hepatocellular Carcinoma and Its Clinical Implication.
Carcinoma, Hepatocellular
Inhibition of DNA primase and induction of apoptosis by 3,3'-diethyl-9-methylthia-carbocyanine iodide in hepatocellular carcinoma BEL-7402 cells.
Herpes Simplex
Herpes Simplex Virus-1 DNA Primase: A Remarkably Inaccurate yet Selective Polymerase.
Herpes Simplex
Herpes simplex virus-1 primase: a polymerase with extraordinarily low fidelity.
Herpes Simplex
Identification and characterization of a DNA primase activity present in herpes simplex virus type 1-infected HeLa cells.
Herpes Simplex
Interaction of herpes primase with the sugar of a NTP.
Herpes Simplex
Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection.
Herpes Simplex
The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein.
Infections
Minute virus of mice-induced modification of the murine DNA polymerase alpha-primase complex permits the salt-induced dissociation of 12S DNA primase and 10S DNA polymerase alpha components.
Infections
Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection.
Leishmaniasis
Evaluation of potential drugs against leishmaniasis targeting catalytic subunit of Leishmania donovani nuclear DNA primase using ligand based virtual screening, docking and molecular dynamics approaches.
Leukemia
Apoptosis induced by DNA primase inhibitor 3,3'-diethyl-9-methylthia-carbocyanine iodide in human leukemia HL-60 cells.
Leukemia
Differential inhibition of various deoxyribonucleic acid polymerases by Evans blue and aurintricarboxylic acid.
Leukemia
Differential inhibition of various deoxyribonucleic and ribonucleic acid polymerases by suramin.
Leukemia
The isolation of a DNA synthesome from human leukemia cells.
Leukemia, Myeloid
Apoptosis induced by DNA primase inhibitor 3,3'-diethyl-9-methylthia-carbocyanine iodide in human leukemia HL-60 cells.
Neoplasms
DNA primase subunit 1 deteriorated progression of hepatocellular carcinoma by activating AKT/mTOR signaling and UBE2C-mediated P53 ubiquitination.
Neoplasms
DNA Primase Subunit 1 Expression in Hepatocellular Carcinoma and Its Clinical Implication.
Neoplasms
Mutation of DNA primase causes extensive apoptosis of retinal neurons through the activation of DNA damage checkpoint and tumor suppressor p53.
Osteosarcoma
Amplifications of DNA primase 1 (PRIM1) in human osteosarcoma.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Inhibition of DNA primase by nucleoside triphosphates and their arabinofuranosyl analogs.
Starvation
Mechanisms of physiological regulation of RNA synthesis in bacteria: new discoveries breaking old schemes.
Tuberculosis
in silico screening and molecular dynamics simulations study to identify novel potent inhibitors against Mycobacterium tuberculosis DnaG primase.
Vaccinia
Products and substrate/template usage of vaccinia virus DNA primase.
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Y155A/Y156A/I157A
mutation reduces PriS binding 1000fold
D101A/D103A
the catalyric site mutant enzyme does not exhibit any detectable catalytic activity, even when higher concentrations of enzyme are utilised. The result demonstrate that the terminal transferase-like activity of PriSL is dependent on the catalytic activity of the primase. D101 and D103 are necessary for PriSL catalytic activity
F164E(PriS)
mutantion in small subunitPriS shows considerably weakened subunit association
F164G/I199K(PriS)_F142E/L163E(PriL)
double mutations of F164G/I199K in small subunit PriS and F142E/L163E in large subunit PriL abolishes the PriS-PriL interaction
G165I(PriS)
mutantion in small subunitPriS shows partial destabilization of the complex
N175A/R176
the affinity of DNA-binding site mutant for NTPs is approximately tenfold lower than that of the wild-type primase and that its enzymatic capability is diminished. Therefore, the mutation of N175 and R176 does not alter the DNA binding properties of the primase but modifies its affinity for free NTPs
R84A/R85A(PriL)
mutation in large subunit shows a marked reduction in the size and amount of RNA product synthesized
D101A/D103A
-
the catalyric site mutant enzyme does not exhibit any detectable catalytic activity, even when higher concentrations of enzyme are utilised. The result demonstrate that the terminal transferase-like activity of PriSL is dependent on the catalytic activity of the primase. D101 and D103 are necessary for PriSL catalytic activity
-
F164E(PriS)
-
mutantion in small subunitPriS shows considerably weakened subunit association
-
F164G/I199K(PriS)_F142E/L163E(PriL)
-
double mutations of F164G/I199K in small subunit PriS and F142E/L163E in large subunit PriL abolishes the PriS-PriL interaction
-
G165I(PriS)
-
mutantion in small subunitPriS shows partial destabilization of the complex
-
N175A/R176
-
the affinity of DNA-binding site mutant for NTPs is approximately tenfold lower than that of the wild-type primase and that its enzymatic capability is diminished. Therefore, the mutation of N175 and R176 does not alter the DNA binding properties of the primase but modifies its affinity for free NTPs
-
R84A/R85A(PriL)
-
mutation in large subunit shows a marked reduction in the size and amount of RNA product synthesized
-
additional information
mutant primase lacking the zinc-binding motifs has higher activity compared with the wild-type enzyme, as well as a bias toward shorter products of 30100 nucleotides
additional information
generation of a PriX deletion mutant that contains amino acid residues 26-154 for crystallization purposes
additional information
-
generation of a PriX deletion mutant that contains amino acid residues 26-154 for crystallization purposes
additional information
-
mutant primase lacking the zinc-binding motifs has higher activity compared with the wild-type enzyme, as well as a bias toward shorter products of 30100 nucleotides
-
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Matsui, E.; Nishio, M.; Yokoyama, H.; Harata, K.; Darnis, S.; Matsui, I.
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14968-14976
2003
Pyrococcus horikoshii (O57934 and O57935), Pyrococcus horikoshii
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Pyrococcus horikoshii (O57934 and O57935)
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Saccharolobus solfataricus (Q9UWW1 and Q97Z83), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q9UWW1 and Q97Z83)
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Pyrococcus horikoshii (O57934 and O57935), Pyrococcus horikoshii
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Pyrococcus furiosus (Q9P9H1 and Q8U4H7), Pyrococcus furiosus
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Thermococcus kodakarensis (Q5JJ72 and Q5JJ73), Thermococcus kodakarensis
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2012
Thermococcus kodakarensis (Q5JJ72 and Q5JJ73), Thermococcus kodakarensis
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344
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2004
Saccharolobus solfataricus (Q9UWW1 and Q97Z83), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q9UWW1 and Q97Z83)
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Le Breton, M.; Henneke, G.; Norais, C.; Flament, D.; Myllykallio, H.; Querellou, J.; Raffin, J.P.
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374
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2007
Pyrococcus abyssi (Q9V292 and Q9V291), Pyrococcus abyssi
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Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
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8
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2001
Pyrococcus furiosus (Q9P9H1 and Q8U4H7)
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Structure of the heterodimeric core primase
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12
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Saccharolobus solfataricus (Q9UWW1 and Q97Z83), Saccharolobus solfataricus P2 (Q9UWW1 and Q97Z83)
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Desogus, G.; Onesti, S.; Brick, P.; Rossi, M.; Pisani, F.M.
Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii
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27
4444-4450
1999
Methanocaldococcus jannaschii (Q58249), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii JAL-1 (Q58249)
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De Falco, M.; Fusco, A.; De Felice, M.; Rossi, M.; Pisani, F.M.
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32
5223-5230
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Saccharolobus solfataricus (Q9UWW1 and Q97Z83), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q9UWW1 and Q97Z83)
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Hu, J.; Guo, L.; Wu, K.; Liu, B.; Lang, S.; Huang, L.
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425
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Saccharolobus solfataricus
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11
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Sulfolobus islandicus
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Beguin, P.; Gill, S.; Charpin, N.; Forterre, P.
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Thermococcus nautili
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Saccharolobus solfataricus (Q9UWW1 AND Q97Z83 AND Q97ZS7), Saccharolobus solfataricus
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