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Literature summary for 2.7.7.B16 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
Search for more literature for 2.7.7.B16

Activating Compound

Activating Compound Comment Organism Structure
additional information PriL but not PriX enhances primer extension by PriS Saccharolobus solfataricus

Cloned(Commentary)

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 (Commentary)

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

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 [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

Metals/Ions Comment Organism Structure
Mn2+ activates Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

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

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

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
archaeal eukaryotic-type primase
-
 Saccharolobus solfataricus
PriL
-
 Saccharolobus solfataricus
PriS
-
 Saccharolobus solfataricus
PriX
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Saccharolobus solfataricus

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharolobus solfataricus

General Information

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 [mM/s]

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