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Literature summary for 2.7.7.B16 extracted from

  • Chemnitz Galal, W.; Pan, M.; Kelman, Z.; Hurwitz, J.
    Characterization of DNA primase complex isolated from the archaeon, Thermococcus kodakaraensis (2012), J. Biol. Chem., 287, 16209-16219.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.B16

Activating Compound

Activating Compound Comment Organism Structure
ATP in the presence of high levels of ATP (ATP:dATP molar ratio of 10:1), dAMP incorporation is stimulated 3-fold, although the size of dAMP-labeled products formed is reduced Thermococcus kodakarensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis

Inhibitors

Inhibitors Comment Organism Structure
dATP synthesis of the short RNA chains is inhibited at all levels of dATP added, and the size of oligo(rA) chains formed and the amount of ATP incorporated are reduced Thermococcus kodakarensis
dGTP dGTP at a molar ratio of dGTP to dATP or rATP of 10:1 inhibits both DNA and RNA synthesis. Lower molar ratios of dGTP:rATP (0.1:1) inhibit ATP incorporation by 91%, whereas dATP incorporation is reduced by 8% Thermococcus kodakarensis
GTP dGTP at a molar ratio of dGTP to dATP or rATP of 10:1 reduces dATP incorporation by 43% and ATP incorporation by 92% Thermococcus kodakarensis
Mn2+ 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+ Thermococcus kodakarensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
 dATP pH 8.0, 60°C, in presence of oligo(dT) Thermococcus kodakarensis
0.04
-
 dATP pH 8.0, 60°C, in presence of ssM13 DNA Thermococcus kodakarensis
0.05
-
 dGTP pH 8.0, 60°C, in presence of oligo(dC) Thermococcus kodakarensis
0.08
-
 ATP pH 8.0, 60°C, in presence of ssM13 DNA Thermococcus kodakarensis
0.09
-
 ATP pH 8.0, 60°C, in presence of oligo(dT) Thermococcus kodakarensis
0.25
-
 GTP pH 8.0, 60°C, in presence of oligo(dC) Thermococcus kodakarensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ 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+ Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JJ72 and Q5JJ73 Q5JJ72: small subunit and Q5JJ73: large subunit
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ATP 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 Thermococcus kodakarensis A(pA)n + n diphosphate
-
 ?
dATP + dATP oligo(dT)30 supports extensive DNA and RNA synthesis Thermococcus kodakarensis dA(pdA)n + n diphosphate
-
 ?
dGTP + n dGTP 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 Thermococcus kodakarensis dG(pdG)n + n diphosphate
-
 ?
dNTP + n dNTP 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 Thermococcus kodakarensis dN(pdN)n + n diphosphate
-
 ?
GTP + n GTP oligo(dC)30 supports extensive DNA and RNA synthesis Thermococcus kodakarensis G(pG)n + n diphosphate
-
 ?
NTP + n NTP 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 Thermococcus kodakarensis N(pN)n + n diphosphate
-
 ?

Subunits

Subunits Comment Organism
heterodimer
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermococcus kodakarensis