Difference between revisions of "AddA"

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(Reviews)
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed>, 20116346 </pubmed>
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<pubmed> 23202527, 20116346 </pubmed>
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==Original publications==
 
==Original publications==
 
'''Additional publications:''' {{PubMed|21071401}}
 
'''Additional publications:''' {{PubMed|21071401}}
 
<pubmed>,8387145,15610857,7746142, 19129187 15009890 10756102 9781875 16632468 17570399 20350930  21809208 21821766 22307084 22383849</pubmed>
 
<pubmed>,8387145,15610857,7746142, 19129187 15009890 10756102 9781875 16632468 17570399 20350930  21809208 21821766 22307084 22383849</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:25, 4 December 2012

  • 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
Get the DNA and protein sequences
(Barbe et al., 2009)
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:

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)

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)


Original publications

Additional publications: PubMed