Difference between revisions of "GuaB"

From SubtiWiki
Jump to: navigation, search
(Extended information on the protein)
(Extended information on the protein)
Line 87: Line 87:
 
* '''Modification:'''  
 
* '''Modification:'''  
 
** phosphorylated (STY) [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
 
** phosphorylated (STY) [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
** S-cysteinlyation after diamide stress (Cys-308) [http://www.ncbi.nlm.nih.gov/pubmed/17611193 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
+
** Cys308 is S-cysteinylated after diamide stress () [http://www.ncbi.nlm.nih.gov/pubmed/17611193 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
** S-bacillithiolated by NaOCl stress on Cys308-SSB in B. subtilis and other Bacillus species [http://www.ncbi.nlm.nih.gov/pubmed/22938038 PubMed]  
+
** Cys308 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species [http://www.ncbi.nlm.nih.gov/pubmed/22938038 PubMed]  
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''

Revision as of 08:10, 6 September 2012

  • Description: IMP dehydrogenase

Gene name guaB
Synonyms guaA
Essential yes PubMed
Product IMP dehydrogenase
Function biosynthesis of GMP
Gene expression levels in SubtiExpress: GuaB
Metabolic function and regulation of this protein in SubtiPathways:
Purine synthesis, Nucleotides (regulation)
MW, pI 52 kDa, 6.168
Gene length, protein length 1464 bp, 488 aa
Immediate neighbours yaaC, dacA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GuaB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GuaB expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, essential genes, phosphoproteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

  • Locus tag: BSU00090

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: Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH (according to Swiss-Prot)
  • Protein family: IMPDH/GMPR family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated (STY) PubMed
    • Cys308 is S-cysteinylated after diamide stress () PubMed, PubMed
    • Cys308 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed
  • Cofactor(s):
  • Effectors of protein activity:
    • inhibition of enzymatic activity by (p)ppGpp during the ´stringent response´PubMed

Database entries

  • Structure: 1VRD (from Thermotoga maritima msb8, 60% identity, 80% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • activated during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information:
    • the mRNA is very stable (half-life > 15 min) PubMed
    • inhibition of enzymatic activity by (p)ppGpp during the ´stringent response´PubMed

Biological materials

  • Mutant:
  • Expression vector:
    • purification from B. subtilis with an N-terminal Strep-tag, for SPINE, (in pGP380): pGP901, available in Stülke lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J Gen Microbiol: 1991, 137(10);2387-94
[PubMed:1722815] [WorldCat.org] [DOI] (P p)

J M Lopez, A Dromerick, E Freese
Response of guanosine 5'-triphosphate concentration to nutritional changes and its significance for Bacillus subtilis sporulation.
J Bacteriol: 1981, 146(2);605-13
[PubMed:6111556] [WorldCat.org] [DOI] (P p)


PubMed