Difference between revisions of "DnaX"
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− | * '''Description:''' DNA polymerase III (gamma and tau subunits) <br/><br/> | + | * '''Description:''' DNA polymerase III (gamma and tau subunits) part of the [[replisome]] <br/><br/> |
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' [[DnaX]]-[[DnaB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14757052 PubMed] | + | * '''Interactions:''' [[DnaX]]-[[DnaB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/14757052 PubMed], part of the [[replisome]]: [[PolC]]-[[HolA]]-[[HolB]]-[[DnaX]]-[[DnaN]]-[[DnaG]]-[[DnaC]]-[[DnaI]]-[[DnaD]]-[[SsbA]]-[[DnaE]]-[[PriA]]-[[DnaB]] {{PubMed|20122408}} |
+ | |||
* '''Localization:''' Nucleoid (Mid-cell) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] nucleoid region (mid-cell spot) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] | * '''Localization:''' Nucleoid (Mid-cell) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] nucleoid region (mid-cell spot) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] | ||
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− | <pubmed> 16479537, 19415803, 14757052, 12974630 1703271, 12466528</pubmed> | + | <pubmed> 16479537, 19415803, 14757052, 12974630 1703271, 12466528 20122408 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:16, 4 February 2010
- 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 |
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 This image was kindly provided by SubtiList
|
Contents
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)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions: DnaX-DnaB PubMed, part of the replisome: PolC-HolA-HolB-DnaX-DnaN-DnaG-DnaC-DnaI-DnaD-SsbA-DnaE-PriA-DnaB PubMed
Database entries
- Structure:
- UniProt: P09122
- KEGG entry: [2]
- E.C. number: 2.7.7.7
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
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)