Difference between revisions of "Sandbox"

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* '''Mutant:'''
 
* '''Mutant:'''
 
** GP1209 (''[[acuC]]''::''kan''), available in [[Stülke]] lab
 
** GP1209 (''[[acuC]]''::''kan''), available in [[Stülke]] lab
** GP1213 (''[[srtN]]''::''cat'')(''[[acuC]]''::''kan''), available in [[Stülke]] lab** 1A887 ( ''acuC''::''spc''), {{PubMed|16855235}}, available at [http://www.bgsc.org/ BGSC]
+
** GP1213 (''[[srtN]]''::''cat'')(''[[acuC]]''::''kan''), available in [[Stülke]] lab** 1A887 ( ''acuC''::''spc''), {{PubMed|16855235}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A887&Search=1A887 BGSC]
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:40, 18 September 2012

Gene name dnaA
Synonyms dnaH, dnaJ, dnaK
Essential yes PubMed
Product replication initiation protein
Function DNA replication
Gene expression levels in SubtiExpress: BSU00010
Interactions involving this protein in SubtInteract: DnaA
MW, pI 50 kDa, 6.035
Gene length, protein length 1338 bp, 446 aa
Immediate neighbours rpmH, dnaN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DnaA dnaN yaaA recF yaaB gyrB context.png
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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Categories containing this gene/protein

DNA replication, essential genes

This gene is a member of the following regulons

Spo0A regulon

The DnaA regulon

The gene

Basic information

  • Locus tag: BSU00010

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:
    • binds multiple regions in the oriC region, required for recruitment of proteins needed to load the replicative helicase DnaC
  • Protein family: dnaA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: AAA+ domain
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • SirA displaces DnaA from the replication origin PubMed
    • YabA inhibits co-operative binding of DnaA to the oriC DNA PubMed
    • DnaA helix formation (and thus replication initiation) is inhibited by the interaction of Soj with the AAA+ domain of DnaA PubMed
    • interaction with DnaD inhibits the ability of DnaA to cooperatively bind to DNA PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Biological materials

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

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)

An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476] [WorldCat.org] [DOI] (I p)

Alan C Leonard, Julia E Grimwade
Regulation of DnaA assembly and activity: taking directions from the genome.
Annu Rev Microbiol: 2011, 65;19-35
[PubMed:21639790] [WorldCat.org] [DOI] (I p)

Alan C Leonard, Julia E Grimwade
Regulating DnaA complex assembly: it is time to fill the gaps.
Curr Opin Microbiol: 2010, 13(6);766-72
[PubMed:21035377] [WorldCat.org] [DOI] (I p)

Tsutomu Katayama, Shogo Ozaki, Kenji Keyamura, Kazuyuki Fujimitsu
Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC.
Nat Rev Microbiol: 2010, 8(3);163-70
[PubMed:20157337] [WorldCat.org] [DOI] (I p)


The DnaA regulon

Alexi I Goranov, Luba Katz, Adam M Breier, Christopher B Burge, Alan D Grossman
A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA.
Proc Natl Acad Sci U S A: 2005, 102(36);12932-7
[PubMed:16120674] [WorldCat.org] [DOI] (P p)

Original publications

Additional publications: PubMed