DnaG_DnaB_bind defines a domain of primase required for functional interaction with DnaB that attracts primase to the replication fork. DnaG_DnaB_bind is responsible for the interaction between DnaG and DnaB.
Eubacterial DnaG primases interact with several factors to form the replisome. One of these factors is DnaB, a helicase. This domain has been demonstrated to be responsible for the interaction between DnaG and DnaB [ (PUBMED:8308039) ]. This domain has a multi-helical structure that forms an orthogonal bundle [ (PUBMED:15649896) ].
GO process:
DNA replication, synthesis of RNA primer (GO:0006269)
There are 5177 DnaG_DnaB_bind domains in 5177 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing DnaG_DnaB_bind domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with DnaG_DnaB_bind domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing DnaG_DnaB_bind domain in the selected taxonomic class.
Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork.
J Biol Chem. 1994; 269: 4675-82
Display abstract
Primase plays a key role in governing the sequence of events required on the lagging strand during a cycle of Okazaki fragment synthesis. To begin to probe the protein-protein interactions necessary for primase function at the replication fork, we have used limited trypsinolysis to separate primase into two functional domains, an N-terminal domain of 49 kDa (p49) and a carboxyl-terminal domain of 16 kDa (p16). p49 retained primase activity in replication assays that utilized bacteriophage M13 DNA carrying the bacteriophage G4 origin of DNA replication as the template, but was inactive during general priming or the conversion of phi X174 single-stranded circular (ss(c))-DNA to the replicative form (RF) and could not support lagging-strand DNA synthesis at replication forks reconstituted with the phi X-type primosomal proteins and the DNA polymerase III holoenzyme. On the other hand, p16 inhibited those replication reactions that included the replication fork helicase, DnaB (general priming, phi X174 ss(c)-->RF, and at the replication fork), but had no effect on those that did not (M13Gori ss(c)-->RF). These results demonstrate that p49 defines a domain of primase required for catalytic activity, that p16 defines a domain of primase required for functional interaction with DnaB, and that it is a protein-protein interaction with DnaB that attracts primase to the replication fork.
Metabolism (metabolic pathways involving proteins which contain this domain)
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with DnaG_DnaB_bind domain which could be assigned to a KEGG orthologous group, and not all proteins containing DnaG_DnaB_bind domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
