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Literature summary for 2.7.7.B17 extracted from

  • Gill, S.; Krupovic, M.; Desnoues, N.; Beguin, P.; Sezonov, G.; Forterre, P.
    A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2 (2014), Nucleic Acids Res., 42, 3707-3719.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.B17

Cloned(Commentary)

Cloned (Comment) Organism
sequence analysis and comparisons of the N-terminal PriS-like domain of PolpTN2 Thermococcus nautili

Protein Variants

Protein Variants Comment Organism
additional information to better understand the functions of the two domains of PolpTN2, a shorter form of this enzyme was engineered by removing the PriL-like domain. The truncated enzyme PolpTN2DELTA311-923 is less susceptible to proteolysis than the native one and retains the DNA polymerase, primase and nucleotidyl transferase activities of the intact protein, confirming that the catalytic activity resides in the N-terminal PriS-like domain. The truncated protein displays a reverse transcriptase activity, which is not observed with the intact enzyme Thermococcus nautili

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermococcus nautili

Organism

Organism UniProt Comment Textmining
Thermococcus nautili
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PolpTN2 exhibits primase, polymerase and nucleotidyl transferase activities and specifically incorporates dNTPs, to the exclusion of rNTPs. It shows strictly dNTP-dependent primase activity of PolpTN2 Thermococcus nautili ?
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 ?

Subunits

Subunits Comment Organism
More the enzyme protein corresponds to a fusion between an N-terminal domain homologous to the small catalytic subunit PriS of heterodimeric archaeal and eukaryotic primases and a C-terminal domain related to their large regulatory subunit PriL. This unique domain configuration is not found in other virus- and plasmid-encoded primases in which PriS-like domains are typically fused to different types of helicases, domain organization of the PolpTN2 primase–polymerase, three-dimensional structure comparisons, overview Thermococcus nautili

Synonyms

Synonyms Comment Organism
archaeo-eukaryotic primase
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 Thermococcus nautili
DNA primase/polymerase protein
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 Thermococcus nautili
PolpTN2
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 Thermococcus nautili

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 primase assay at Thermococcus nautili

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 primase assay at Thermococcus nautili

General Information

General Information Comment Organism
evolution PolpTN2 is indeed formed by the association of an N-terminal DNA polymerase/primase domain and a C-terminal domain whose sequences bear a distant similarity to the catalytic and regulatory subunits, respectively, of heterodimeric (PriS-PriL) archaeal and eukaryotic primases. The N-terminal domain possesses reverse transcriptase activity this activity can reflect an ancestral function of archaeal and eukaryotic primases proteins in the transition from the RNA to the DNA world Thermococcus nautili
physiological function PolpTN2 exhibits DNA polymerase, DNA primase and nucleotidyl terminal transferase activities. PolpTN2 can efficiently prime DNA synthesis by cellular DNA polymerases, suggesting that this protein is used in vivo as primase for pTN2 plasmid replication. The PriL-like domain enhances the stringency of PolpTN2 polymerase. The N-terminal PriS-like domain of PolpTN2 exhibits all activities of the full-length enzyme but is much less efficient in priming cellular DNA polymerases. The N-terminal domain possesses reverse transcriptase activity Thermococcus nautili