AddB

• Description: ATP-dependent deoxyribonuclease (subunit B)
  
  

Gene name	addB
Synonyms
Essential	no
Product	ATP-dependent deoxyribonuclease (subunit B))
Function	DNA repair and recombination
MW, pI	134 kDa, 5.39
Gene length, protein length	3498 bp, 1166 aa
Immediate neighbours	yhjR, addA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU10620

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• 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

• Structure: 1Y26 (the riboswitch in complex with adenine)

• UniProt: P23477

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: addB-addA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • positive control by ComK PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP1106 (addAB, spc), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

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

Natali Fili, Gregory I Mashanov, Christopher P Toseland, Christopher Batters, Mark I Wallace, Joseph T P Yeeles, Mark S Dillingham, Martin R Webb, Justin E Molloy
Visualizing helicases unwinding DNA at the single molecule level.
Nucleic Acids Res: 2010, 38(13);4448-57
[PubMed:20350930] [WorldCat.org] [DOI] (I p)

Joseph T P Yeeles, Richard Cammack, Mark S Dillingham
An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases.
J Biol Chem: 2009, 284(12);7746-55
[PubMed:19129187] [WorldCat.org] [DOI] (P p)

Joseph T P Yeeles, Mark S Dillingham
A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases.
J Mol Biol: 2007, 371(1);66-78
[PubMed:17570399] [WorldCat.org] [DOI] (P p)

Alexander Serganov, Yu-Ren Yuan, Olga Pikovskaya, Anna Polonskaia, Lucy Malinina, Anh Tuân Phan, Claudia Hobartner, Ronald Micura, Ronald R Breaker, Dinshaw J Patel
Structural basis for discriminative regulation of gene expression by adenine- and guanine-sensing mRNAs.
Chem Biol: 2004, 11(12);1729-41
[PubMed:15610857] [WorldCat.org] [DOI] (P p)

F Chédin, S D Ehrlich, S C Kowalczykowski
The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro.
J Mol Biol: 2000, 298(1);7-20
[PubMed:10756102] [WorldCat.org] [DOI] (P p)

F Chédin, P Noirot, V Biaudet, S D Ehrlich
A five-nucleotide sequence protects DNA from exonucleolytic degradation by AddAB, the RecBCD analogue of Bacillus subtilis.
Mol Microbiol: 1998, 29(6);1369-77
[PubMed:9781875] [WorldCat.org] [DOI] (P p)

B J Haijema, L W Hamoen, J Kooistra, G Venema, D van Sinderen
Expression of the ATP-dependent deoxyribonuclease of Bacillus subtilis is under competence-mediated control.
Mol Microbiol: 1995, 15(2);203-11
[PubMed:7746142] [WorldCat.org] [DOI] (P p)

J Kooistra, B J Haijema, G Venema
The Bacillus subtilis addAB genes are fully functional in Escherichia coli.
Mol Microbiol: 1993, 7(6);915-23
[PubMed:8387145] [WorldCat.org] [DOI] (P p)

J Kooistra, G Venema
Cloning, sequencing, and expression of Bacillus subtilis genes involved in ATP-dependent nuclease synthesis.
J Bacteriol: 1991, 173(12);3644-55
[PubMed:1646786] [WorldCat.org] [DOI] (P p)