Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | PriL but not PriX enhances primer extension by PriS | Saccharolobus solfataricus |
Cloned (Comment) | Organism |
---|---|
genes priL, priS, and SSO0502, DNA and amino acid sequence determination and analysis of PriX, phylogenetic analysis and tree, recombinant expression of a deletion mutant PriX protein containing amino acid residues 26-154 | Saccharolobus solfataricus |
Crystallization (Comment) | Organism |
---|---|
purified recombinant PriX deletion mutant 26-154, X-ray diffraction strutcure determination and analysis at 1.95 A resolution, crystallization of the full-length PriX is unsuccessful | Saccharolobus solfataricus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of a PriX deletion mutant that contains amino acid residues 26-154 for crystallization purposes | Saccharolobus solfataricus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0032 | - |
NTP | recombinant PriSLX, pH 6.5, 55°C | Saccharolobus solfataricus | |
0.0141 | - |
NTP | recombinant PriSX, pH 6.5, 55°C | Saccharolobus solfataricus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates | Saccharolobus solfataricus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dNTP + n dNTP | Saccharolobus solfataricus | - |
dN(pdN)n + n diphosphate | - |
? | |
NTP + n NTP | Saccharolobus solfataricus | - |
N(pN)n + n diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | Q9UWW1 AND Q97Z83 AND Q97ZS7 | subunits PriL, PriS, and PriX; genes priL, priS, and SSO0502 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dGTP + n dGTP | the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation | Saccharolobus solfataricus | dG(pdG)n + n diphosphate | - |
? | |
dNTP + n dNTP | - |
Saccharolobus solfataricus | dN(pdN)n + n diphosphate | - |
? | |
GTP + n GTP | the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation | Saccharolobus solfataricus | G(pG)n + n diphosphate | - |
? | |
additional information | usage of M13mp18ssDNA as a template | Saccharolobus solfataricus | ? | - |
? | |
NTP + n NTP | - |
Saccharolobus solfataricus | N(pN)n + n diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotrimer | archaea encode a eukaryotic-type primase comprising a catalytic subunit, PriS, and a noncatalytic subunit, PriL and PriX. PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron-sulfur cluster. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. PriL, but not PriX, facilitates primer extension by PriS. The catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis. PriX subunit residues 26-54 are in a flexible region. PriX residues 55-154 fold into a single domain containing 6 helices, which form a compact core stabilized by extensive hydrophobic interactions. The overall structure of the PriX protein is quite unique, sequence and three-dimensional structure comparisons, overview | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
archaeal eukaryotic-type primase | - |
Saccharolobus solfataricus |
PriL | - |
Saccharolobus solfataricus |
PriS | - |
Saccharolobus solfataricus |
PriX | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Saccharolobus solfataricus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.011 | - |
NTP | recombinant PriSX, pH 6.5, 55°C | Saccharolobus solfataricus | |
0.022 | - |
NTP | recombinant PriSLX, pH 6.5, 55°C | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Saccharolobus solfataricus |
General Information | Comment | Organism |
---|---|---|
evolution | the majority of primases are classified into two major groups, that is, the bacterial DnaG-type primases and the more complex eukaryotic primases. Archaea encode both types of DNA primase, they encode a eukaryotic-type primase comprising a catalytic subunit (PriS) and a noncatalytic subunit (PriL). Identification of a primase noncatalytic subunit, termed PriX, from the hyperthermophilic archaeon Sulfolobus solfataricus. Phylogenomic analysis, overview | Saccharolobus solfataricus |
additional information | the catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis. The catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis. PriX subunit residues 26-54 are in a flexible region. PriX residues 55-154 fold into a single domain containing 6 helices, which form a compact core stabilized by extensive hydrophobic interactions. The overall structure of the PriX protein is quite unique | Saccharolobus solfataricus |
physiological function | DNA primases play a critical role in the initiation of DNA replication by synthesizing RNA primers on both the leading and lagging strands since DNA polymerases are incapable of de novo DNA synthesis. Product synthesis by PriSL in the presence of PriX, the Sso0502 product, is over an order of magnitude (about 16fold) more efficient than that in its absence. PriX and PriL bind template DNA differently. Both PriSX and PriSLX differ from PriSL in primer synthesis, overview. PriL but not PriX enhances primer extension by PriS | Saccharolobus solfataricus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0000013 | - |
NTP | recombinant PriSL, pH 6.5, 55°C | Saccharolobus solfataricus | |
0.00078 | - |
NTP | recombinant PriSX, pH 6.5, 55°C | Saccharolobus solfataricus | |
0.0068 | - |
NTP | recombinant PriSLX, pH 6.5, 55°C | Saccharolobus solfataricus |