Difference between revisions of "GyrB"

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(Extended information on the protein)
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* '''Modification:''' phosphorylatd on Ser-400 {{PubMed|20509597}}
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* '''Modification:''' phosphorylated on Ser-400 {{PubMed|20509597}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''

Revision as of 08:00, 3 June 2010

  • Description: DNA-Gyrase (subunit B)

Gene name gyrB
Synonyms novA
Essential yes PubMed
Product DNA-Gyrase (subunit B)
Function DNA supercoiling,
initation of replication cycle and DNA elongation
MW, pI 71 kDa, 5.378
Gene length, protein length 1914 bp, 638 aa
Immediate neighbours yaaB, gyrA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DnaA dnaN yaaA recF yaaB gyrB context.png
This image was kindly provided by SubtiList




The gene

Basic information

  • Locus tag: BSU00060

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA (according to Swiss-Prot)
  • Protein family: type II topoisomerase family (according to Swiss-Prot)
  • Paralogous protein(s): ParE

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on Ser-400 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: nucleoid-associated in actively growing cells PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information: GyrB is subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Dagmar Klostermeier, Biozentrum Basel, Switzerland homepage

Your additional remarks

References

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Airat Gubaev, Manuel Hilbert, Dagmar Klostermeier
The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction.
Proc Natl Acad Sci U S A: 2009, 106(32);13278-83
[PubMed:19666507] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Thomas Göttler, Dagmar Klostermeier
Dissection of the nucleotide cycle of B. subtilis DNA gyrase and its modulation by DNA.
J Mol Biol: 2007, 367(5);1392-404
[PubMed:17320901] [WorldCat.org] [DOI] (P p)

W M Huang, J L Libbey, P van der Hoeven, S X Yu
Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme required for chromosome segregation.
Proc Natl Acad Sci U S A: 1998, 95(8);4652-7
[PubMed:9539793] [WorldCat.org] [DOI] (P p)

N Ogasawara, S Moriya, H Yoshikawa
Structure and function of the region of the replication origin of the Bacillus subtilis chromosome. IV. Transcription of the oriC region and expression of DNA gyrase genes and other open reading frames.
Nucleic Acids Res: 1985, 13(7);2267-79
[PubMed:2987848] [WorldCat.org] [DOI] (P p)