Difference between revisions of "PolX"
Line 125: | Line 125: | ||
** 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 14:12, 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28590
Phenotypes of a mutant
Database entries
- BsubCyc: BSU28590
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- 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
Database entries
- BsubCyc: BSU28590
- Structure:
- UniProt: P94544
- KEGG entry: [2]
- E.C. number: 2.7.7.7
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)