Difference between revisions of "AddA"

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(Original publications)
(Reviews)
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed> 23202527, 20116346 22933559</pubmed>
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<pubmed> 23202527, 20116346 22933559 19542287 </pubmed>
  
 
==Original publications==
 
==Original publications==
 
<pubmed>,8387145,15610857,7746142, 19129187 15009890 10756102 9781875 16632468 17570399 20350930  21809208 21821766 22307084 24682829 24670664 22383849 21071401 8752329 8752323 </pubmed>
 
<pubmed>,8387145,15610857,7746142, 19129187 15009890 10756102 9781875 16632468 17570399 20350930  21809208 21821766 22307084 24682829 24670664 22383849 21071401 8752329 8752323 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:06, 26 June 2014

  • Description: ATP-dependent deoxyribonuclease (subunit A)

Gene name addA
Synonyms recE5
Essential no
Product ATP-dependent deoxyribonuclease (subunit A))
Function DNA repair/ recombination
Gene expression levels in SubtiExpress: addA
Interactions involving this protein in SubtInteract: AddA
MW, pI 140 kDa, 5.127
Gene length, protein length 3696 bp, 1232 aa
Immediate neighbours addB, sbcD
Sequences Protein DNA DNA_with_flanks
Genetic context
AddA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AddA expression.png















Categories containing this gene/protein

DNA repair/ recombination, genetic competence

This gene is a member of the following regulons

ComK regulon

The gene

Basic information

  • Locus tag: BSU10630

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed


The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • the enzyme is functional as a heterodimer of the AddA and AddB subunits, that it is a rapid and processive DNA helicase, and that it catalyses DNA unwinding using one single-stranded DNA motor of 3'→5' polarity located in the AddA subunit PubMed
    • the AddB subunit contains a second putative ATP-binding pocket, but this does not contribute to the observed helicase activity and may instead be involved in the recognition of recombination hotspot sequences PubMed
  • Protein family: uvrD-like helicase C-terminal domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 147 PubMed

Biological materials

  • Mutant: GP1106 (addAB, spc), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Dale B Wigley
Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB.
Nat Rev Microbiol: 2013, 11(1);9-13
[PubMed:23202527] [WorldCat.org] [DOI] (I p)

Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559] [WorldCat.org] [DOI] (I p)

Joseph T P Yeeles, Mark S Dillingham
The processing of double-stranded DNA breaks for recombinational repair by helicase-nuclease complexes.
DNA Repair (Amst): 2010, 9(3);276-85
[PubMed:20116346] [WorldCat.org] [DOI] (I p)

Gareth A Cromie
Phylogenetic ubiquity and shuffling of the bacterial RecBCD and AddAB recombination complexes.
J Bacteriol: 2009, 191(16);5076-84
[PubMed:19542287] [WorldCat.org] [DOI] (I p)


Original publications