Difference between revisions of "SdhB"

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(Biological materials)
(Biological materials)
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* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
* '''GFP fusion:'''
+
* '''GFP fusion:''' GP1436 (spc, based on [[pGP1870]]), available in the [[Stülke]] lab
  
 
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
 
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab

Revision as of 09:36, 2 November 2012

  • Description: succinate dehydrogenase

Gene name sdhB
Synonyms
Essential no
Product succinate dehydrogenase (iron-sulfur protein)
Function TCA cycle
Gene expression levels in SubtiExpress: sdhB
Interactions involving this protein in SubtInteract: SdhB
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 28 kDa, 7.989
Gene length, protein length 759 bp, 253 aa
Immediate neighbours ysmA, sdhA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SdhB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdhB expression.png




























Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

FsrA regulon

The gene

Basic information

  • Locus tag: BSU28430

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Succinate + acceptor = fumarate + reduced acceptor (according to Swiss-Prot)
  • Protein family: succinate dehydrogenase/fumarate reductase iron-sulfur protein family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): Fe
  • Effectors of protein activity:
    • Inhibited by 2-(n-Heptyl)-4-hydroxy-quinoline N-oxide PubMed
    • Activated by Cytochrome b558 PubMed

Database entries

  • Structure: 1NEK (E. coli)
  • KEGG entry: [3]
  • E.C. number:EC 1.3.99.1

Additional information

  • This enzyme is a trimer membrane-bound PubMed PubMed
    • One subunit is bound to citochrome b558, and this subunit is the one bound to the cytosolic side of the membrane PubMed PubMed
    • Another subunit is the flavoprotein one, required for FAD usage PubMed PubMed
    • The other subunit has an iron-sulphur domain necessary for the catalytic activity PubMed PubMed
  • extensive information on the structure and enzymatic properties of succinate dehydrogenase can be found at Proteopedia

Expression and regulation

  • Regulation: constitutive
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion: GP1436 (spc, based on pGP1870), available in the Stülke lab
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:
  • FLAG-tag construct: GP1426 (spc, based on pGP1331), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J. Bacteriol.: 2012, 194(10);2594-605
[PubMed:22389480] [WorldCat.org] [DOI] (I p)

Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth, César Luna-Chavez, Hideto Miyoshi, Christophe Léger, Bernadette Byrne, Gary Cecchini, So Iwata
Architecture of succinate dehydrogenase and reactive oxygen species generation.
Science: 2003, 299(5607);700-4
[PubMed:12560550] [WorldCat.org] [DOI] (I p)

C Hägerhäll, V Sled, L Hederstedt, T Ohnishi
The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties.
Biochim. Biophys. Acta: 1995, 1229(3);356-62
[PubMed:7748886] [WorldCat.org] [DOI] (P p)

C Hägerhäll, R Aasa, C von Wachenfeldt, L Hederstedt
Two hemes in Bacillus subtilis succinate:menaquinone oxidoreductase (complex II).
Biochemistry: 1992, 31(32);7411-21
[PubMed:1324713] [WorldCat.org] [DOI] (P p)

L Melin, H Fridén, E Dehlin, L Rutberg, A von Gabain
The importance of the 5'-region in regulating the stability of sdh mRNA in Bacillus subtilis.
Mol. Microbiol.: 1990, 4(11);1881-9
[PubMed:1707123] [WorldCat.org] (P p)

L Melin, L Rutberg, A von Gabain
Transcriptional and posttranscriptional control of the Bacillus subtilis succinate dehydrogenase operon.
J. Bacteriol.: 1989, 171(4);2110-5
[PubMed:2495271] [WorldCat.org] [DOI] (P p)

A AEvarsson, L Hederstedt
Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase.
FEBS Lett.: 1988, 232(2);298-302
[PubMed:2837411] [WorldCat.org] [DOI] (P p)

L Melin, K Magnusson, L Rutberg
Identification of the promoter of the Bacillus subtilis sdh operon.
J. Bacteriol.: 1987, 169(7);3232-6
[PubMed:3036777] [WorldCat.org] [DOI] (P p)

M K Phillips, L Hederstedt, S Hasnain, L Rutberg, J R Guest
Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex.
J. Bacteriol.: 1987, 169(2);864-73
[PubMed:3027051] [WorldCat.org] [DOI] (P p)

S T Cole, C Condon, B D Lemire, J H Weiner
Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli.
Biochim. Biophys. Acta: 1985, 811(4);381-403
[PubMed:3910107] [WorldCat.org] [DOI] (P p)

L Hederstedt, L Rutberg
Orientation of succinate dehydrogenase and cytochrome b558 in the Bacillus subtilis cytoplasmic membrane.
J. Bacteriol.: 1983, 153(1);57-65
[PubMed:6401289] [WorldCat.org] (P p)

L Hederstedt, L Rutberg
Succinate dehydrogenase--a comparative review.
Microbiol. Rev.: 1981, 45(4);542-55
[PubMed:6799760] [WorldCat.org] (P p)