Difference between revisions of "Ung"

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|style="background:#ABCDEF;" align="center"|'''Function''' || DNA repair  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || DNA repair  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU37970 ung]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Ung Ung]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Ung Ung]

Revision as of 17:10, 7 August 2012

  • 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
Get the DNA and protein sequences
(Barbe et al., 2009)
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

Additional publications: PubMed

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)

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)