AddA

• Description: ATP-dependent deoxyribonuclease (subunit A), required for efficient survival and replication restart after replication-transcription conflicts
  
  

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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• recO addA-addB double mutants are extremely sensitive against DNA damaging agents PubMed

Database entries

• BsubCyc: BSU10630

• 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:

• Interactions:
  • AddA-AddB PubMed

• Localization:

Database entries

• BsubCyc: BSU10630

• Structure: 3U4Q (the AddA-AddB-DNA complex) PubMed

• UniProt: P23478

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: addB-addA-sbcD-sbcC-hlpB PubMed

• Expression browser: addA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • positive control by ComK PubMed

• Regulatory mechanism:

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

Biological materials

• Mutant: GP1106 (addA-addB, spc), available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Mark Dillingham, Bristol, U.K. (homepage)

References

Reviews

Martin Wilkinson, Dale B Wigley
Structural features of Chi recognition in AddAB with implications for RecBCD.
Cell Cycle: 2014, 13(18);2812-20
[PubMed:25486468] [WorldCat.org] [DOI] (I p)

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)