Difference between revisions of "Nfo"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 262 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 262 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 659 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 659 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 612 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 355 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 628 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''  
 
* '''Mutant:'''  
 
** available in [[Mario Pedraza-Reyes]]' lab
 
** available in [[Mario Pedraza-Reyes]]' lab

Revision as of 14:20, 17 April 2014

  • Description: type IV apurinic/apyrimidinic endonuclease

Gene name nfo
Synonyms yqfS
Essential no
Product type IV apurinic/apyrimidinic endonuclease
Function repair of oxidative DNA damage in spores
Gene expression levels in SubtiExpress: nfo
MW, pI 32 kDa, 5.371
Gene length, protein length 891 bp, 297 aa
Immediate neighbours yqfT, cshB
Sequences Protein DNA DNA_with_flanks
Genetic context
YqfS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Nfo expression.png















Categories containing this gene/protein

DNA repair/ recombination, sporulation proteins

This gene is a member of the following regulons

SigG regulon

The gene

Basic information

  • Locus tag: BSU25130

Phenotypes of a mutant

  • an exoA nfo double mutant is impaired in germination and spore outgrowth due to the accumulation of DNA lesions, this can be rescued by inactivation of disA PubMed
  • an exoA nfo double mutant is sensitive to radiation PubMed

Database entries

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

Additional information

  • Nfo is functionally redundant with ExoA

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products (according to Swiss-Prot)
  • Protein family: AP endonuclease 2 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • expressed late during sporulation in the forespore (SigG) PubMed
  • Regulatory mechanism:
  • Additional information:

The gene yqfT is located between nfo and yqfU, but is transcribed in the opposite direction.

    • number of protein molecules per cell (minimal medium with glucose and ammonium): 262 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 659 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 612 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 355 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 628 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Silvia S Campos, Juan R Ibarra-Rodriguez, Rocío C Barajas-Ornelas, Fernando H Ramírez-Guadiana, Armando Obregón-Herrera, Peter Setlow, Mario Pedraza-Reyes
Interaction of apurinic/apyrimidinic endonucleases Nfo and ExoA with the DNA integrity scanning protein DisA in the processing of oxidative DNA damage during Bacillus subtilis spore outgrowth.
J Bacteriol: 2014, 196(3);568-78
[PubMed:24244006] [WorldCat.org] [DOI] (I p)

Ralf Moeller, Marina Raguse, Günther Reitz, Ryuichi Okayasu, Zuofeng Li, Stuart Klein, Peter Setlow, Wayne L Nicholson
Resistance of Bacillus subtilis spore DNA to lethal ionizing radiation damage relies primarily on spore core components and DNA repair, with minor effects of oxygen radical detoxification.
Appl Environ Microbiol: 2014, 80(1);104-9
[PubMed:24123749] [WorldCat.org] [DOI] (I p)

Ralf Moeller, Peter Setlow, Mario Pedraza-Reyes, Ryuichi Okayasu, Günther Reitz, Wayne L Nicholson
Role of the Nfo and ExoA apurinic/apyrimidinic endonucleases in radiation resistance and radiation-induced mutagenesis of Bacillus subtilis spores.
J Bacteriol: 2011, 193(11);2875-9
[PubMed:21441501] [WorldCat.org] [DOI] (I p)

Marcelo Barraza-Salas, Juan R Ibarra-Rodríguez, Silvia J Mellado, José M Salas-Pacheco, Peter Setlow, Mario Pedraza-Reyes
Effects of forespore-specific overexpression of apurinic/apyrimidinic endonuclease Nfo on the DNA-damage resistance properties of Bacillus subtilis spores.
FEMS Microbiol Lett: 2010, 302(2);159-65
[PubMed:19930460] [WorldCat.org] [DOI] (I p)

Juan R Ibarra, Alma D Orozco, Juan A Rojas, Karina López, Peter Setlow, Ronald E Yasbin, Mario Pedraza-Reyes
Role of the Nfo and ExoA apurinic/apyrimidinic endonucleases in repair of DNA damage during outgrowth of Bacillus subtilis spores.
J Bacteriol: 2008, 190(6);2031-8
[PubMed:18203828] [WorldCat.org] [DOI] (I p)

José M Salas-Pacheco, Barbara Setlow, Peter Setlow, Mario Pedraza-Reyes
Role of the Nfo (YqfS) and ExoA apurinic/apyrimidinic endonucleases in protecting Bacillus subtilis spores from DNA damage.
J Bacteriol: 2005, 187(21);7374-81
[PubMed:16237020] [WorldCat.org] [DOI] (P p)

José M Salas-Pacheco, Norma Urtiz-Estrada, Guadalupe Martínez-Cadena, Ronald E Yasbin, Mario Pedraza-Reyes
YqfS from Bacillus subtilis is a spore protein and a new functional member of the type IV apurinic/apyrimidinic-endonuclease family.
J Bacteriol: 2003, 185(18);5380-90
[PubMed:12949090] [WorldCat.org] [DOI] (P p)

Norma Urtiz-Estrada, José M Salas-Pacheco, Ronald E Yasbin, Mario Pedraza-Reyes
Forespore-specific expression of Bacillus subtilis yqfS, which encodes type IV apurinic/apyrimidinic endonuclease, a component of the base excision repair pathway.
J Bacteriol: 2003, 185(1);340-8
[PubMed:12486072] [WorldCat.org] [DOI] (P p)