Difference between revisions of "AddB"

From SubtiWiki
Jump to: navigation, search
m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
Line 105: Line 105:
 
* '''Operon:''' ''[[addB]]-[[addA]]'' {{PubMed|1646786}}  
 
* '''Operon:''' ''[[addB]]-[[addA]]'' {{PubMed|1646786}}  
  
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|7746142}}  
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=addB_1136320_1139820_1 addB] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:''' [[SigA]] {{PubMed|7746142}}  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 112: Line 114:
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
* '''Additional information:'''  
+
* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =

Revision as of 17:23, 12 April 2012

  • Description: ATP-dependent deoxyribonuclease (subunit B)

Gene name addB
Synonyms
Essential no
Product ATP-dependent deoxyribonuclease (subunit B))
Function DNA repair/ recombination
Interactions involving this protein in SubtInteract: AddB
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
AddB context.gif
This image was kindly provided by SubtiList





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: BSU10620

Phenotypes of a mutant

Database entries

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

Additional information

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

Original publications

Additional publications: PubMed

Natalia Fili, Christopher P Toseland, Mark S Dillingham, Martin R Webb, Justin E Molloy
A single-molecule approach to visualize the unwinding activity of DNA helicases.
Methods Mol Biol: 2011, 778;193-214
[PubMed:21809208] [WorldCat.org] [DOI] (I p)

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)