Difference between revisions of "SdhA"

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* '''Mutant:''' GP743 (''sdhCA'', cat), available in [[Stülke]] lab
 
* '''Mutant:''' GP743 (''sdhCA'', cat), available in [[Stülke]] lab
 +
** GP792 (''sdhCAB''::''phleo''), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:08, 13 August 2013

  • Description: succinate dehydrogenase (flavoprotein subunit)

Gene name sdhA
Synonyms citF
Essential no
Product succinate dehydrogenase (flavoprotein subunit)
Function TCA cycle
Gene expression levels in SubtiExpress: sdhA
Interactions involving this protein in SubtInteract: SdhA
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 65 kDa, 5.714
Gene length, protein length 1758 bp, 586 aa
Immediate neighbours sdhB, sdhC
Sequences Protein DNA DNA_with_flanks
Genetic context
SdhA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdhA expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins

This gene is a member of the following regulons

FsrA regulon

The gene

Basic information

  • Locus tag: BSU28440

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: FRD/SDH subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • 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: 1.3.99.1

Additional information

  • This enzyme is a membrane-bound trimer PubMed PubMed
    • One subunit is bound to cytochrome 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
    • part of the iron sparing response (FsrA) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP743 (sdhCA, cat), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Lars Hederstedt
Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis.
Biochim. Biophys. Acta: 2002, 1553(1-2);74-83
[PubMed:11803018] [WorldCat.org] [DOI] (P p)

Original publications

Pedro M F Sousa, Marco A M Videira, Filipe A S Santos, Brian L Hood, Thomas P Conrads, Ana M P Melo
The bc:caa3 supercomplexes from the Gram positive bacterium Bacillus subtilis respiratory chain: a megacomplex organization?
Arch. Biochem. Biophys.: 2013, 537(1);153-60
[PubMed:23880299] [WorldCat.org] [DOI] (I p)

Juri Niño Bach, Marc Bramkamp
Flotillins functionally organize the bacterial membrane.
Mol. Microbiol.: 2013, 88(6);1205-17
[PubMed:23651456] [WorldCat.org] [DOI] (I p)

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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

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)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P 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, 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] [DOI] (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)

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)

K Magnusson, L Hederstedt, L Rutberg
Cloning and expression in Escherichia coli of sdhA, the structural gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex.
J. Bacteriol.: 1985, 162(3);1180-5
[PubMed:2987185] [WorldCat.org] [DOI] (P p)

L Hederstedt
Succinate dehydrogenase mutants of Bacillus subtilis lacking covalently bound flavin in the flavoprotein subunit.
Eur. J. Biochem.: 1983, 132(3);589-93
[PubMed:6406223] [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] [DOI] (P p)

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