The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

sdhC  -  succinate dehydrogenase, membrane subunit,...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0710, JW0711, cybA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of sdhC


High impact information on sdhC

  • An increase in cytochrome b content was found in the membrane when sdhD was introduced, while the cytochrome b content did not change when sdhC was introduced [1].
  • To understand how ArcA participates in the anaerobic repression of sdhCDAB expression, a family of sdhC-lacZ fusions was constructed and analysed in vivo [3].
  • Lastly, the Fnr-dependent control of sdhCDAB gene expression was shown to occur independently of the ArcA and to require DNA sequences near the start of sdhC transcription [3].
  • A base-pair exchange of G to A in the ribosome-binding sequence of sdhC was found to reduce cytochrome b-558 translation about tenfold in B. subtilis, whereas the mutation had no effect on translation in E. coli [4].
  • From the result of steady-state kinetics of cytochromes in the membrane and E'm values of purified cytochromes, we propose a branched arrangement of the late exponential phase of aerobic growth, as shown in Fig. 10. Cytochrome b-556 is reduced by several dehydrogenases and the gene for this cytochrome (cybA) is located in the sdh gene cluster [5].

Biological context of sdhC

  • The sdhC (384 base-pairs) and sdhD (342 base-pairs) structural genes encode two strongly hydrophobic proteins of Mr 14167 and 12792 respectively [6].
  • Lastly, sdhC-lacZ expression was shown to vary with the cell growth rate during aerobic and anaerobic conditions [7].
  • There is little homology between the B. subtilis cytochrome b558 and cytochrome b of mitochondrial complex III from different organisms or between cytochrome b558 and the hydrophobic sdhC and sdhD peptides of the Escherichia coli sdh operon [8].

Associations of sdhC with chemical compounds

  • In contrast, significantly higher amounts of cytochrome b556 were expressed in the membrane when sdhC and sdhD genes were both present, and the catalytic portion was found to be localized in the membrane with succinate-ubiquitnone oxidoreductase and succinate oxidase activities [1].
  • Together with data showing correlation between the intracellular cAMP concentrations and the sdhC-lacZ expression levels in several mutants and wild type, in vitro transcription assays suggest that the decrease in the CRP.cAMP level in the presence of glucose is the major determinant of the glucose repression of the sdhCDAB operon [9].

Other interactions of sdhC

  • Iron and haem availability affected sdhC-lacZ expression by two- to three-fold [7].


  1. Two hydrophobic subunits are essential for the heme b ligation and functional assembly of complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli. Nakamura, K., Yamaki, M., Sarada, M., Nakayama, S., Vibat, C.R., Gennis, R.B., Nakayashiki, T., Inokuchi, H., Kojima, S., Kita, K. J. Biol. Chem. (1996) [Pubmed]
  2. Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase. Immunochemistry, cloning, and nucleotide sequencing. Yu, L., Wei, Y.Y., Usui, S., Yu, C.A. J. Biol. Chem. (1992) [Pubmed]
  3. Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB) gene expression in Escherichia coli. Shen, J., Gunsalus, R.P. Mol. Microbiol. (1997) [Pubmed]
  4. Genetic and biochemical characterization of Bacillus subtilis mutants defective in expression and function of cytochrome b-558. Fridén, H., Rutberg, L., Magnusson, K., Hederstedt, L. Eur. J. Biochem. (1987) [Pubmed]
  5. Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain. Kita, K., Konishi, K., Anraku, Y. Meth. Enzymol. (1986) [Pubmed]
  6. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Wood, D., Darlison, M.G., Wilde, R.J., Guest, J.R. Biochem. J. (1984) [Pubmed]
  7. Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr. Park, S.J., Tseng, C.P., Gunsalus, R.P. Mol. Microbiol. (1995) [Pubmed]
  8. Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex. Magnusson, K., Philips, M.K., Guest, J.R., Rutberg, L. J. Bacteriol. (1986) [Pubmed]
  9. Glucose repression of the Escherichia coli sdhCDAB operon, revisited: regulation by the CRP*cAMP complex. Nam, T.W., Park, Y.H., Jeong, H.J., Ryu, S., Seok, Y.J. Nucleic Acids Res. (2005) [Pubmed]
WikiGenes - Universities