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Gene Review

SDH2  -  succinate dehydrogenase iron-sulfur...

Saccharomyces cerevisiae S288c

Synonyms: Ip, Iron-sulfur subunit of complex II, SDH, SDHB, YLL041C
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High impact information on SDH2

  • Genetic synthetic interaction experiments confirmed a functional relationship between YFH1 and succinate dehydrogenase genes SDH1 and SDH2 [1].
  • One FAD and three iron-sulfur clusters were docked into the Sdh1p and Sdh2p catalytic dimer [2].
  • For example, the steady state levels of SDH2 mRNA and SUC2 mRNA are significantly determined by their differential rates of turnover [3].
  • Isolation and characterization of a Saccharomyces cerevisiae mutant with a disrupted gene for the IP subunit of succinate dehydrogenase [4].
  • SDH2 mRNA has a very short half-life in medium with glucose (YPD) and a significantly longer half-life in medium with glycerol (YPG) [5].

Biological context of SDH2


Anatomical context of SDH2

  • In mitochondria, MPP may recognize the stretched polyprotein during passage of the precursor through the translocational apparatus in the inner membrane, and cleave the connecting region between the SDHB and RPS14 domains even before processing of the presequence [7].

Associations of SDH2 with chemical compounds

  • The membrane extrinsic domain, consisting of Sdh1p and Sdh2p, contains a covalent FAD cofactor and three iron-sulfur clusters [8].
  • A discovery made originally with the transcript of the SDH2 gene prompted an investigation of post-transcriptional mechanisms, and more specifically a study of the turnover rate of this mRNA in the absence and presence of glucose [5].


  1. Frataxin interacts functionally with mitochondrial electron transport chain proteins. González-Cabo, P., Vázquez-Manrique, R.P., García-Gimeno, M.A., Sanz, P., Palau, F. Hum. Mol. Genet. (2005) [Pubmed]
  2. The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies. Oyedotun, K.S., Lemire, B.D. J. Biol. Chem. (2004) [Pubmed]
  3. Glucose-regulated turnover of mRNA and the influence of poly(A) tail length on half-life. Prieto, S., de la Cruz, B.J., Scheffler, I.E. J. Biol. Chem. (2000) [Pubmed]
  4. Isolation and characterization of a Saccharomyces cerevisiae mutant with a disrupted gene for the IP subunit of succinate dehydrogenase. Lombardo, A., Scheffler, I.E. J. Biol. Chem. (1989) [Pubmed]
  5. Control of mRNA turnover as a mechanism of glucose repression in Saccharomyces cerevisiae. Scheffler, I.E., de la Cruz, B.J., Prieto, S. Int. J. Biochem. Cell Biol. (1998) [Pubmed]
  6. The carboxyl terminus of the Saccharomyces cerevisiae succinate dehydrogenase membrane subunit, SDH4p, is necessary for ubiquinone reduction and enzyme stability. Oyedotun, K.S., Lemire, B.D. J. Biol. Chem. (1997) [Pubmed]
  7. Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase. Oshima, T., Yamasaki, E., Ogishima, T., Kadowaki, K., Ito, A., Kitada, S. Biochem. J. (2005) [Pubmed]
  8. The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II). Dibrov, E., Fu, S., Lemire, B.D. J. Biol. Chem. (1998) [Pubmed]
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