Difference between revisions of "PolX"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 199 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 199 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 540 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 540 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 92 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 101 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 258 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 15:12, 17 April 2014

  • Description: DNA polymerase X, involved in DNA repair

Gene name polX
Synonyms yshC
Essential no
Product DNA polymerase X
Function DNA repair
Gene expression levels in SubtiExpress: polX
MW, pI 63 kDa, 5.308
Gene length, protein length 1710 bp, 570 aa
Immediate neighbours mutSB, yshB
Sequences Protein DNA DNA_with_flanks
Genetic context
YshC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PolX expression.png
























Categories containing this gene/protein

DNA repair/ recombination

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU28590

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • template-dependent DNA polymerase, fills single nucleotide gaps PubMed
    • has intrinsic 3'-5' exonuclease activity for resecting unannealed 3'-termini in gapped DNA substrates PubMed
    • has intrinsic apurinic/apyrimidinic (AP) endonuclease activity PubMed
  • Protein family: DNA polymerase X family
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 199 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 540 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 92 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 101 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 258 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Margarita Salas, Madrid, Spain link

Your additional remarks

References

Reviews

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)

Original publications

Benito Baños, Laurentino Villar, Margarita Salas, Miguel de Vega
DNA stabilization at the Bacillus subtilis PolX core--a binding model to coordinate polymerase, AP-endonuclease and 3'-5' exonuclease activities.
Nucleic Acids Res: 2012, 40(19);9750-62
[PubMed:22844091] [WorldCat.org] [DOI] (I p)

Benito Baños, Laurentino Villar, Margarita Salas, Miguel de Vega
Intrinsic apurinic/apyrimidinic (AP) endonuclease activity enables Bacillus subtilis DNA polymerase X to recognize, incise, and further repair abasic sites.
Proc Natl Acad Sci U S A: 2010, 107(45);19219-24
[PubMed:20974932] [WorldCat.org] [DOI] (I p)

Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Characterization of a Bacillus subtilis 64-kDa DNA polymerase X potentially involved in DNA repair.
J Mol Biol: 2008, 384(5);1019-28
[PubMed:18938175] [WorldCat.org] [DOI] (I p)

Benito Baños, José M Lázaro, Laurentino Villar, Margarita Salas, Miguel de Vega
Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase.
Nucleic Acids Res: 2008, 36(18);5736-49
[PubMed:18776221] [WorldCat.org] [DOI] (I p)