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Literature summary for 2.7.7.101 extracted from

  • Bogutzki, A.; Naue, N.; Litz, L.; Pich, A.; Curth, U.
    E. coli primase and DNA polymerase III holoenzyme are able to bind concurrently to a primed template during DNA replication (2019), Sci. Rep., 9, 14460 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.101

Cloned(Commentary)

Cloned (Comment) Organism
gene dnaG, recombinant enzyme expression in Escherichia coli Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABS5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 binding assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 binding assay at Escherichia coli

General Information

General Information Comment Organism
additional information using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB, it is tested whether DnaG and pol III can bind concurrently to the primed template. The binding of both proteins to SSB is mutually exclusive. Using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB. Both primase and the chi subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB). About 10 nucleotides have to be added in order to displace one of the two primase molecules bound to SSB-saturated G4ori, specific binding of DnaG primase to G4ori. In a ssM13Gori replication system, DNA polymerase III holoenzyme does not displace primase from ssM13Gori. After primer synthesis in the absence of CTP, half of the primase is displaced from ssM13Gori/SSB by an addition of pol III and dTTP, dGTP and dCTP. Only the mixture of dTTP, dGTP and dCTP causes significant primase dissociation: about half of the enzyme is released from the complex Escherichia coli
physiological function during DNA replication in Escherichia coli, a switch between DnaG primase and DNA polymerase III holoenzyme (pol III) activities has to occur every time when the synthesis of a new Okazaki fragment starts. As both primase and the chi subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB), it is proposed that the binding of both proteins to SSB is mutually exclusive. The addition of pol III does not lead to a displacement of primase, but to the formation of higher complexes. Even pol III-mediated primer elongation by one or several DNA nucleotides does not result in the dissociation of DnaG. The concurrent binding of primase and pol III is highly plausible, since even the SSB tetramer situated directly next to the 3'-terminus of the primer provides four C-termini for protein-protein interactions Escherichia coli