DnaG

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  • 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
DnaG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DnaG expression.png















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]

Additional information

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

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
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

Labs working on this gene/protein

Your additional remarks

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)