Difference between revisions of "DnaB"

From SubtiWiki
Jump to: navigation, search
Line 29: Line 29:
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaB_2964148_2965566_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:dnaB_expression.png|500px]]
+
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=dnaB_2964148_2965566_-1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:dnaB_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28990]]
 
|-
 
|-
 
|}
 
|}

Revision as of 14:14, 16 May 2013

  • Description: initiation of chromosome replication/ membrane attachment protein, part of the replisome

Gene name dnaB
Synonyms
Essential yes PubMed
Product initiation of chromosome replication/ membrane attachment protein
Function DNA replication
Gene expression levels in SubtiExpress: dnaB
Interactions involving this protein in SubtInteract: DnaB
MW, pI 54 kDa, 5.278
Gene length, protein length 1416 bp, 472 aa
Immediate neighbours dnaI, ytcG
Sequences Protein DNA DNA_with_flanks
Genetic context
DnaB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DnaB 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: BSU28990

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:
  • 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]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

Reviews

Original publications

Wiep Klaas Smits, Houra Merrikh, Carla Yaneth Bonilla, Alan D Grossman
Primosomal proteins DnaD and DnaB are recruited to chromosomal regions bound by DnaA in Bacillus subtilis.
J Bacteriol: 2011, 193(3);640-8
[PubMed:21097613] [WorldCat.org] [DOI] (I p)

Farhat Y Marston, William H Grainger, Wiep Klaas Smits, Nicholas H Hopcroft, Matthew Green, Andrea M Hounslow, Alan D Grossman, C Jeremy Craven, Panos Soultanas
When simple sequence comparison fails: the cryptic case of the shared domains of the bacterial replication initiation proteins DnaB and DnaD.
Nucleic Acids Res: 2010, 38(20);6930-42
[PubMed:20587500] [WorldCat.org] [DOI] (I p)

S Moriya, R A Rashid, C D Andrade Rodrigues, E J Harry
Influence of the nucleoid and the early stages of DNA replication on positioning the division site in Bacillus subtilis.
Mol Microbiol: 2010, 76(3);634-47
[PubMed:20199598] [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)

William H Grainger, Cristina Machón, David J Scott, Panos Soultanas
DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(9);2851-64
[PubMed:20071750] [WorldCat.org] [DOI] (I p)

Wiep Klaas Smits, Alexi I Goranov, Alan D Grossman
Ordered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo.
Mol Microbiol: 2010, 75(2);452-61
[PubMed:19968790] [WorldCat.org] [DOI] (I p)

Megan E Rokop, Alan D Grossman
Intragenic and extragenic suppressors of temperature sensitive mutations in the replication initiation genes dnaD and dnaB of Bacillus subtilis.
PLoS One: 2009, 4(8);e6774
[PubMed:19707554] [WorldCat.org] [DOI] (I e)

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)

Claude Bruand, Marion Velten, Stephen McGovern, Stéphanie Marsin, Céline Sérèna, S Dusko Ehrlich, Patrice Polard
Functional interplay between the Bacillus subtilis DnaD and DnaB proteins essential for initiation and re-initiation of DNA replication.
Mol Microbiol: 2005, 55(4);1138-50
[PubMed:15686560] [WorldCat.org] [DOI] (P p)

Megan E Rokop, Jennifer M Auchtung, Alan D Grossman
Control of DNA replication initiation by recruitment of an essential initiation protein to the membrane of Bacillus subtilis.
Mol Microbiol: 2004, 52(6);1757-67
[PubMed:15186423] [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)

Marion Velten, Stephen McGovern, Stéphanie Marsin, S Dusko Ehrlich, Philippe Noirot, Patrice Polard
A two-protein strategy for the functional loading of a cellular replicative DNA helicase.
Mol Cell: 2003, 11(4);1009-20
[PubMed:12718886] [WorldCat.org] [DOI] (P p)

P Soultanas
A functional interaction between the putative primosomal protein DnaI and the main replicative DNA helicase DnaB in Bacillus.
Nucleic Acids Res: 2002, 30(4);966-74
[PubMed:11842108] [WorldCat.org] [DOI] (I p)

C Bruand, M Farache, S McGovern, S D Ehrlich, P Polard
DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome.
Mol Microbiol: 2001, 42(1);245-55
[PubMed:11679082] [WorldCat.org] [DOI] (P p)

S Marsin, S McGovern, S D Ehrlich, C Bruand, P Polard
Early steps of Bacillus subtilis primosome assembly.
J Biol Chem: 2001, 276(49);45818-25
[PubMed:11585815] [WorldCat.org] [DOI] (P p)

M Bárcena, T Ruiz, L E Donate, S E Brown, N E Dixon, M Radermacher, J M Carazo
The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel.
EMBO J: 2001, 20(6);1462-8
[PubMed:11250911] [WorldCat.org] [DOI] (P p)

Y Imai, N Ogasawara, D Ishigo-Oka, R Kadoya, T Daito, S Moriya
Subcellular localization of Dna-initiation proteins of Bacillus subtilis: evidence that chromosome replication begins at either edge of the nucleoids.
Mol Microbiol: 2000, 36(5);1037-48
[PubMed:10844689] [WorldCat.org] [DOI] (P p)

G Henckes, F Harper, A Levine, F Vannier, S J Séror
Overreplication of the origin region in the dnaB37 mutant of Bacillus subtilis: postinitiation control of chromosomal replication.
Proc Natl Acad Sci U S A: 1989, 86(22);8660-4
[PubMed:2554322] [WorldCat.org] [DOI] (P p)