Difference between revisions of "DnaX"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** [[DnaX]]-[[DnaB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14757052 PubMed]
 
** [[DnaX]]-[[DnaB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14757052 PubMed]
 +
** [[DnaX]]-[[DnaC]] {{PubMed|23525462}}
 +
** [[DnaX]](3)-[[YqeN]]-[[HolB]], the clamp-loader complex {{PubMed|23525462}}
 
** part of the [[replisome]]: [[PolC]]-[[HolA]]-[[HolB]]-[[DnaX]]-[[DnaN]]-[[DnaG]]-[[DnaC]]-[[DnaI]]-[[DnaD]]-[[SsbA]]-[[DnaE]]-[[PriA]]-[[DnaB]] {{PubMed|20122408}}
 
** part of the [[replisome]]: [[PolC]]-[[HolA]]-[[HolB]]-[[DnaX]]-[[DnaN]]-[[DnaG]]-[[DnaC]]-[[DnaI]]-[[DnaD]]-[[SsbA]]-[[DnaE]]-[[PriA]]-[[DnaB]] {{PubMed|20122408}}
  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaX_26814_28505_1 dnaX] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaX_26814_28505_1 dnaX] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
'''Additional publications:''' {{PubMed|23268446,21958350}}
+
<pubmed> 16479537, 19415803, 14757052, 12974630 1703271, 12466528 20122408 23525462 23268446,21958350</pubmed>
<pubmed> 16479537, 19415803, 14757052, 12974630 1703271, 12466528 20122408 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:15, 27 March 2013

  • Description: DNA polymerase III (gamma and tau subunits) part of the replisome

Gene name dnaX
Synonyms dnaH, dna-8132
Essential yes PubMed
Product DNA polymerase III (gamma and tau subunits)
Function DNA replication
Gene expression levels in SubtiExpress: dnaX
Interactions involving this protein in SubtInteract: DnaX
MW, pI 62 kDa, 5.488
Gene length, protein length 1689 bp, 563 aa
Immediate neighbours scr, yaaK
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DnaX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DnaX expression.png















Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00190

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) (according to Swiss-Prot)
    • required for bacteriophage SPP1 replication PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

José P Afonso, Kiran Chintakayala, Chatrudee Suwannachart, Svetlana Sedelnikova, Kevin Giles, John B Hoyes, Panos Soultanas, John B Rafferty, Neil J Oldham
Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase.
Nucleic Acids Res: 2013, 41(9);5115-26
[PubMed:23525462] [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)

Andrew D Klocko, Jeremy W Schroeder, Brian W Walsh, Justin S Lenhart, Margery L Evans, Lyle A Simmons
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.
Mol Microbiol: 2011, 82(3);648-63
[PubMed:21958350] [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)

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)

Anna Haroniti, Christopher Anderson, Zara Doddridge, Laurence Gardiner, Clive J Roberts, Stephanie Allen, Panos Soultanas
The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus.
J Mol Biol: 2004, 336(2);381-93
[PubMed:14757052] [WorldCat.org] [DOI] (P p)

A Haroniti, R Till, M C M Smith, P Soultanas
Clamp-loader-helicase interaction in Bacillus. Leucine 381 is critical for pentamerization and helicase binding of the Bacillus tau protein.
Biochemistry: 2003, 42(37);10955-64
[PubMed:12974630] [WorldCat.org] [DOI] (P p)

María I Martínez-Jiménez, Pablo Mesa, Juan C Alonso
Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P.
Nucleic Acids Res: 2002, 30(23);5056-64
[PubMed:12466528] [WorldCat.org] [DOI] (I p)

J C Struck, J C Alonso, H Y Toschka, V A Erdmann
The Bacillus subtilis small cytoplasmic RNA gene and 'dnaX' map near the chromosomal replication origin.
Mol Gen Genet: 1990, 222(2-3);470-2
[PubMed:1703271] [WorldCat.org] [DOI] (P p)