Difference between revisions of "YabA"

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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
+
* '''Operon:''' ''[[yaaQ]]-[[yaaR]]-[[holB]]-[[yaaT]]-[[yabA]]-[[yabB]]-[[yazA]]-[[yabC]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yabA_42499_42858_1 yabA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yabA_42499_42858_1 yabA] {{PubMed|22383849}}
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<pubmed> 20157337 </pubmed>
 
<pubmed> 20157337 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed> 19578359, 21895792,12060778 16461910, 19737352 19081080 23909787 </pubmed>
+
<pubmed> 19578359, 21895792,12060778 16461910, 19737352 19081080 23909787 22383849</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:25, 27 November 2013

  • Description: inhibitor of DnaA oligomerization, tethers DnaA to the polymerase-clamp protein DnaN

Gene name yabA
Synonyms
Essential no
Product negative regulator of replication initiation
Function positioning of DnaA
Gene expression levels in SubtiExpress: yabA
Interactions involving this protein in SubtInteract: YabA
MW, pI 13 kDa, 6.065
Gene length, protein length 357 bp, 119 aa
Immediate neighbours yaaT, yabB
Sequences Protein DNA DNA_with_flanks
Genetic context
YabA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YabA expression.png















Categories containing this gene/protein

DNA replication

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00330

Phenotypes of a mutant

strongly reduced growth rate in minimal medium PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • negative control of replication initiation PubMed
    • associates with the oriC region in a DnaA-dependent manner, this limits the amount of DnaA that can bind the oriC region PubMed
    • YabA inhibits co-operative DNA binding by DnaA PubMed
    • inhibits oligomerization and helix formation of DnaA PubMed
  • Protein family: yabA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: leucine zipper
  • Modification:
  • Cofactor(s): Zn cluster
  • Effectors of protein activity:
    • DnaN overexpression or release from the replisome decreases association of YabA with oriC, increases association of DnaA with oriC PubMed

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Philippe Noirot, Jouy-en-Josas, France Homepage
Alan Grossman, Cambridge, MA, USA Homepage

Your additional remarks

References

Reviews

Original publications

Graham Scholefield, Heath Murray
YabA and DnaD inhibit helix assembly of the DNA replication initiation protein DnaA.
Mol Microbiol: 2013, 90(1);147-59
[PubMed:23909787] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Houra Merrikh, Alan D Grossman
Control of the replication initiator DnaA by an anti-cooperativity factor.
Mol Microbiol: 2011, 82(2);434-46
[PubMed:21895792] [WorldCat.org] [DOI] (I p)

Alexi I Goranov, Adam M Breier, Houra Merrikh, Alan D Grossman
YabA of Bacillus subtilis controls DnaA-mediated replication initiation but not the transcriptional response to replication stress.
Mol Microbiol: 2009, 74(2);454-66
[PubMed:19737352] [WorldCat.org] [DOI] (I p)

Avigdor Eldar, Vasant K Chary, Panagiotis Xenopoulos, Michelle E Fontes, Oliver C Losón, Jonathan Dworkin, Patrick J Piggot, Michael B Elowitz
Partial penetrance facilitates developmental evolution in bacteria.
Nature: 2009, 460(7254);510-4
[PubMed:19578359] [WorldCat.org] [DOI] (I p)

Clarisse Defeu Soufo, Hervé Joël Defeu Soufo, Marie-Françoise Noirot-Gros, Astrid Steindorf, Philippe Noirot, Peter L Graumann
Cell-cycle-dependent spatial sequestration of the DnaA replication initiator protein in Bacillus subtilis.
Dev Cell: 2008, 15(6);935-41
[PubMed:19081080] [WorldCat.org] [DOI] (I p)

Marie-Françoise Noirot-Gros, M Velten, M Yoshimura, S McGovern, T Morimoto, S D Ehrlich, N Ogasawara, P Polard, Philippe Noirot
Functional dissection of YabA, a negative regulator of DNA replication initiation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2006, 103(7);2368-73
[PubMed:16461910] [WorldCat.org] [DOI] (P p)

Marie-Françoise Noirot-Gros, Etienne Dervyn, Ling Juan Wu, Peggy Mervelet, Jeffery Errington, S Dusko Ehrlich, Philippe Noirot
An expanded view of bacterial DNA replication.
Proc Natl Acad Sci U S A: 2002, 99(12);8342-7
[PubMed:12060778] [WorldCat.org] [DOI] (P p)