PolX

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

Categories containing this gene/protein

DNA repair/ recombination

The gene

Basic information

• Locus tag: BSU28590

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • monomeric PubMed

• Localization:

Database entries

• Structure:

• UniProt: P94544

• KEGG entry: [2]

• E.C. number: 2.7.7.7

Expression and regulation

• Operon:

• Expression browser: polX PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Margarita Salas, Madrid, Spain link

References

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)