DnaG is a bacterial DNA primase and is encoded by the dnaG gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis.

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DnaA is the specialist initiator protein that recognizes the origin and guides the formation of these nucleoprotein complexes [92–94]. To initiate DNA replication, this complex must be activated and undergo large conformational changes that result in the local unwinding of duplex DNA.

2017年4月6日 · To better understand the structure and function of primase and address the interactions between DnaG and specific DNA template, we have carried out structural and functional analysis on DnaG...

2019年10月8日 · In E. coli, the hexameric helicase (DnaB), primase (DnaG), single-stranded DNA-binding protein (SSB) and DNA polymerase III holoenzyme (pol III) as the replicative DNA polymerase are necessary...

Compounds that inhibit bacterial DnaG primase have been developed using different approaches. In this paper, we provide an overview of the current literature on DNA primases as novel drug targets and the methods used to find their inhibitors.

2007年10月19日 · DnaG increases both the NTPase and the helicase activities of DnaB (9), and DnaB both increases and modulates the synthesis of RNA primers by DnaG (1). DnaG consists of three domains, an N-terminal zinc-binding domain (ZBD), an RNA polymerase domain (RPD), and a C-terminal HBD.

DnaG is a bacterial DNA primase and is encoded by the dnaG gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis.

In Escherichia coli, the primase (DnaG) transcribes ~2000 to 3000 RNA primers per replication cycle5. Biochemical studies have demonstrated that the DnaG primase initiates primer synthesis on...

The bacterial primase (DnaG)–helicase (DnaB) interaction is mediated by the C-terminal domain of DnaG (p16) and a linker that joins the N- and C-terminal domains (p17 and p33 respectively) of DnaB.