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Literature summary extracted from

  • Monachino, E.; Jergic, S.; Lewis, J.S.; Xu, Z.Q.; Lo, A.T.Y.; O'Shea, V.L.; Berger, J.M.; Dixon, N.E.; van Oijen, A.M.
    A primase-induced conformational switch controls the stability of the bacterial replisome (2020), Mol. Cell, 79, 140-154.e7 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.101 DnaB analysis of the DnaB N-terminal domain structure and conformations, with or without bound DNA, kinetics. In a crystal structure of the Geobacillus stearothermophilus DnaB6-(DnaGC)3 complex, the three C-terminal domains of primase each bind to two adjacent subunits of the dilated N-tier of DnaB. Binding of primase does not inhibit DnaB helicase activity Geobacillus stearothermophilus
2.7.7.101 DnaB interaction with the replisome, overview. Analysis of the DnaB N-terminal domain structure and conformations, with or without bound DNA, kinetics. Binding of primase does not inhibit DnaB helicase activity Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.101 ssDNA + n NTP Geobacillus stearothermophilus
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Escherichia coli
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.101 Escherichia coli P0ABS5
-
-
2.7.7.101 Geobacillus stearothermophilus Q9X4D0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.101 ssDNA + n NTP
-
 Geobacillus stearothermophilus ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Escherichia coli ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.101 More in a crystal structure of the Geobacillus stearothermophilus DnaB6-(DnaGC)3 complex, the three C-terminal domains of primase each bind to two adjacent subunits of the dilated N-tier of DnaB Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.101 DnaG
-
 Geobacillus stearothermophilus
2.7.7.101 DnaG
-
 Escherichia coli
2.7.7.101 DnaG primase
-
 Geobacillus stearothermophilus
2.7.7.101 DnaG primase
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.101 metabolism CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview Geobacillus stearothermophilus
2.7.7.101 metabolism CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview Escherichia coli
2.7.7.101 physiological function the primase-induced conformational switch controls the stability of the bacterial replisome. The dynamic interaction of the Escherichia coli DnaG primase and DnaB helicase affects the stability of the replisome and the cycling of DNA polymerase III complexes at the replication fork through a conformational switch in DnaB that toggles its affinity for the polymerase. Molecular mechanism for polymerase exchange and revised model for the replication reaction that emphasizes its stochasticity, overview. DnaG stimulates polymerase accumulation and slows its exchange at the replication fork Geobacillus stearothermophilus
2.7.7.101 physiological function the primase-induced conformational switch controls the stability of the bacterial replisome. The dynamic interaction of the Escherichia coli DnaG primase and DnaB helicase affects the stability of the replisome and the cycling of DNA polymerase III complexes at the replication fork through a conformational switch in DnaB that toggles its affinity for the polymerase. Molecular mechanism for polymerase exchange and revised model for the replication reaction that emphasizes its stochasticity, overview. DnaG stimulates polymerase accumulation and slows its exchange at the replication fork Escherichia coli