DnaG

• Description: DNA primase, part of the replisome
  
  

Gene name	dnaG
Synonyms	dnaE
Essential	yes PubMed
Product	DNA primase
Function	DNA replication
MW, pI	68 kDa, 6.706
Gene length, protein length	1809 bp, 603 aa
Immediate neighbours	sigA, antE
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU25210

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Categories containing this gene/protein

DNA replication, essential genes

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: DNA primase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: the enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed

• Interactions: part of the replisome: PolC-HolA-HolB-DnaX-DnaN-DnaG-DnaC-DnaI-DnaD-SsbA-DnaE-PriA-DnaB PubMed

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure: 1D0Q (zinc binding domain, Geobacillus stearothermophilus), 1Z8S (DnaB binding domain, AA 452-597, Geobacillus stearothermophilus)

• UniProt: P05096

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yqxD-dnaG-sigA PubMed

• Sigma factor: SigA PubMed, SigBPubMed, SigH PubMed

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed

• Additional information:
  • enzymatic activity is inhibited by (p)ppGpp during the ´stringent response´ PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Glenn M Sanders, H Garry Dallmann, Charles S McHenry
Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases.
Mol Cell: 2010, 37(2);273-81
[PubMed:20122408] [WorldCat.org] [DOI] (I p)

Kiran Chintakayala, Cristina Machón, Anna Haroniti, Marilyn A Larson, Steven H Hinrichs, Mark A Griep, Panos Soultanas
Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.
Mol Microbiol: 2009, 72(2);537-49
[PubMed:19415803] [WorldCat.org] [DOI] (I p)

Jue D Wang, Glenn M Sanders, Alan D Grossman
Nutritional control of elongation of DNA replication by (p)ppGpp.
Cell: 2007, 128(5);865-75
[PubMed:17350574] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

L F Wang, C W Price, R H Doi
Bacillus subtilis dnaE encodes a protein homologous to DNA primase of Escherichia coli.
J Biol Chem: 1985, 260(6);3368-72
[PubMed:3919021] [WorldCat.org] (P p)