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Literature summary for 2.7.7.101 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
Search for more literature for 2.7.7.101

Activating Compound

Activating Compound Comment Organism Structure
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
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)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABS5
-
-
Geobacillus stearothermophilus Q9X4D0
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
DnaG
-
 Geobacillus stearothermophilus
DnaG
-
 Escherichia coli
DnaG primase
-
 Geobacillus stearothermophilus
DnaG primase
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview Geobacillus stearothermophilus
metabolism CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview Escherichia coli
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
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