Nfo

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

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

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:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P54476

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: nfo-yqfU PubMed

• Expression browser: nfo PubMed

• Sigma factor: SigG PubMed

• 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.

Biological materials

• Mutant:
  • available in Mario Pedraza-Reyes' lab
  • GP899 (nfo::kan) and GP1502 (nfo::cat), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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

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)