DnaG

• Description: DNA primase, part of the replisome
  
  

Gene name	dnaG
Synonyms	dnaE
Essential	yes PubMed
Product	DNA primase
Function	DNA replication
Gene expression levels in SubtiExpress: dnaG
Interactions involving this protein in SubtInteract: DnaG
MW, pI	68 kDa, 6.706
Gene length, protein length	1809 bp, 603 aa
Immediate neighbours	sigA, antE
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

SigH regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU25210

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • required for bacteriophage SPP1 replication PubMed

• 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
  • DnaG primase activity is stimulates by DnaC PubMed

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

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure:
  • 1D0Q (zinc binding domain, Geobacillus stearothermophilus)
  • 1Z8S (DnaB binding domain, AA 452-597, Geobacillus stearothermophilus)
  • 4M4W (the DnaC-DnaI-DnaG complex) PubMed

• UniProt: P05096

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yqxD-dnaG-sigA PubMed

• Expression browser: dnaG PubMed

• Sigma factor: SigA PubMed, 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

Reviews

Geoffrey S Briggs, Wiep Klaas Smits, Panos Soultanas
Chromosomal replication initiation machinery of low-G+C-content Firmicutes.
J Bacteriol: 2012, 194(19);5162-70
[PubMed:22797751] [WorldCat.org] [DOI] (I p)

Richard L Gourse, James L Keck
Magic spots cast a spell on DNA primase.
Cell: 2007, 128(5);823-4
[PubMed:17350566] [WorldCat.org] [DOI] (P p)

Original publications

Bin Liu, William K Eliason, Thomas A Steitz
Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.
Nat Commun: 2013, 4;2495
[PubMed:24048025] [WorldCat.org] [DOI] (I p)

Olivier Rannou, Emmanuelle Le Chatelier, Marilynn A Larson, Hamid Nouri, Bérengère Dalmais, Charles Laughton, Laurent Jannière, Panos Soultanas
Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.
Nucleic Acids Res: 2013, 41(10);5303-20
[PubMed:23563155] [WorldCat.org] [DOI] (I p)

Elena M Seco, John C Zinder, Carol M Manhart, Ambra Lo Piano, Charles S McHenry, Silvia Ayora
Bacteriophage SPP1 DNA replication strategies promote viral and disable host replication in vitro.
Nucleic Acids Res: 2013, 41(3);1711-21
[PubMed:23268446] [WorldCat.org] [DOI] (I p)

Masayuki Su'etsugu, Jeff Errington
The replicase sliding clamp dynamically accumulates behind progressing replication forks in Bacillus subtilis cells.
Mol Cell: 2011, 41(6);720-32
[PubMed:21419346] [WorldCat.org] [DOI] (I p)

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)