Difference between revisions of "Ung"

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* increased mutation rates {{PubMed|22056936}}
 
* increased mutation rates {{PubMed|22056936}}
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37970&redirect=T BSU37970]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ung.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ung.html]
Line 93: Line 94:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU37970&redirect=T BSU37970]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3A7N 3A7N] (from ''Mycobacterium tuberculosis'', 42% identity) {{PubMed|20693660}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3A7N 3A7N] (from ''Mycobacterium tuberculosis'', 42% identity) {{PubMed|20693660}}

Revision as of 15:07, 2 April 2014

  • Description: uracil-DNA glycosylase

Gene name ung
Synonyms ipa-57d, ywdG
Essential no
Product uracil-DNA glycosylase
Function DNA repair
Gene expression levels in SubtiExpress: ung
Interactions involving this protein in SubtInteract: Ung
MW, pI 25 kDa, 8.782
Gene length, protein length 675 bp, 225 aa
Immediate neighbours ywdH, ywdF
Sequences Protein DNA DNA_with_flanks
Genetic context
Ung context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Ung 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: BSU37970

Phenotypes of a mutant

  • increased mutation rates PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: removes uracil preferentially from single-stranded DNA over double-stranded DNA, exhibiting higher preference for U:G than U:A mismatches PubMed
  • Protein family: uracil-DNA glycosylase 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: 3A7N (from Mycobacterium tuberculosis, 42% identity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • expressed throughout growth and staionary phase PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

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

Karina López-Olmos, Martha P Hernández, Jorge A Contreras-Garduño, Eduardo A Robleto, Peter Setlow, Ronald E Yasbin, Mario Pedraza-Reyes
Roles of endonuclease V, uracil-DNA glycosylase, and mismatch repair in Bacillus subtilis DNA base-deamination-induced mutagenesis.
J Bacteriol: 2012, 194(2);243-52
[PubMed:22056936] [WorldCat.org] [DOI] (I p)

Laura Pérez-Lago, Gemma Serrano-Heras, Benito Baños, José M Lázaro, Martín Alcorlo, Laurentino Villar, Margarita Salas
Characterization of Bacillus subtilis uracil-DNA glycosylase and its inhibition by phage φ29 protein p56.
Mol Microbiol: 2011, 80(6);1657-66
[PubMed:21542855] [WorldCat.org] [DOI] (I p)

Audrey Costes, François Lecointe, Stephen McGovern, Sophie Quevillon-Cheruel, Patrice Polard
The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks.
PLoS Genet: 2010, 6(12);e1001238
[PubMed:21170359] [WorldCat.org] [DOI] (I e)

Prem Singh Kaushal, Ramappa K Talawar, Umesh Varshney, M Vijayan
Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis: insights into interactions with ligands.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 8);887-92
[PubMed:20693660] [WorldCat.org] [DOI] (I p)

E Presecan, I Moszer, L Boursier, H Cruz Ramos, V de la Fuente, M-F Hullo, C Lelong, S Schleich, A Sekowska, B H Song, G Villani, F Kunst, A Danchin, P Glaser
The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).
Microbiology (Reading): 1997, 143 ( Pt 10);3313-3328
[PubMed:9353933] [WorldCat.org] [DOI] (P p)