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

• The hydrophilic subunits, SDH1p and SDH2p, comprise the catalytic domain involved in succinate oxidation [6].

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].

References