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Literature summary extracted from

  • Liu, B.; Ouyang, S.; Makarova, K.S.; Xia, Q.; Zhu, Y.; Li, Z.; Guo, L.; Koonin, E.V.; Liu, Z.J.; Huang, L.
    A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase (2015), Nat. Commun., 6, 7300.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.B16 additional information PriL but not PriX enhances primer extension by PriS Saccharolobus solfataricus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.B16 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 (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.B16 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

EC Number Protein Variants Comment Organism
2.7.7.B16 additional information generation of a PriX deletion mutant that contains amino acid residues 26-154 for crystallization purposes Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.B16 0.0032
-
 NTP recombinant PriSLX, pH 6.5, 55°C Saccharolobus solfataricus
2.7.7.B16 0.0141
-
 NTP recombinant PriSX, pH 6.5, 55°C Saccharolobus solfataricus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.B16 Mn2+ activates Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.B16 dNTP + n dNTP Saccharolobus solfataricus
-
 dN(pdN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP Saccharolobus solfataricus
-
 N(pN)n + n diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.B16 Saccharolobus solfataricus Q9UWW1 AND Q97Z83 AND Q97ZS7 subunits PriL, PriS, and PriX; genes priL, priS, and SSO0502
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.B16 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
-
 ?
2.7.7.B16 dNTP + n dNTP
-
 Saccharolobus solfataricus dN(pdN)n + n diphosphate
-
 ?
2.7.7.B16 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
-
 ?
2.7.7.B16 additional information usage of M13mp18ssDNA as a template Saccharolobus solfataricus ?
-
 ?
2.7.7.B16 NTP + n NTP
-
 Saccharolobus solfataricus N(pN)n + n diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.B16 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

EC Number Synonyms Comment Organism
2.7.7.B16 archaeal eukaryotic-type primase
-
 Saccharolobus solfataricus
2.7.7.B16 PriL
-
 Saccharolobus solfataricus
2.7.7.B16 PriS
-
 Saccharolobus solfataricus
2.7.7.B16 PriX
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.B16 55
-
-
 Saccharolobus solfataricus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.B16 0.011
-
 NTP recombinant PriSX, pH 6.5, 55°C Saccharolobus solfataricus
2.7.7.B16 0.022
-
 NTP recombinant PriSLX, pH 6.5, 55°C Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.B16 6.5
-
 assay at Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
2.7.7.B16 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
2.7.7.B16 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
2.7.7.B16 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.7.B16 0.0000013
-
 NTP recombinant PriSL, pH 6.5, 55°C Saccharolobus solfataricus
2.7.7.B16 0.00078
-
 NTP recombinant PriSX, pH 6.5, 55°C Saccharolobus solfataricus
2.7.7.B16 0.0068
-
 NTP recombinant PriSLX, pH 6.5, 55°C Saccharolobus solfataricus