High impact information on SDH1

• One FAD and three iron-sulfur clusters were docked into the Sdh1p and Sdh2p catalytic dimer [1].
• We now show that the SDH1 and SUC2 5'UTRs are capable of conferring glucose-sensitive mRNA instability [2].
• The absence of detectable succinate dehydrogenase activity in mitochondria of E264/U2 and the lack of complementation of the mutant by an sdh11null strain indicated a mutation in SDH1 [3].
• One of the plasmids (pG52/T3) contained SDH1 coding for the flavoprotein subunit of mitochondrial succinate dehydrogenase [3].
• Sequence analysis revealed that most of the remaining regulated fusions are in new yeast genes, while some are in previously characterized yeast genes (PTP1, RPM2, SDH1) [4].

Biological context of SDH1

• The hydrophilic subunits, SDH1p and SDH2p, comprise the catalytic domain involved in succinate oxidation [5].
• The expression of the two genes was compared by assaying the beta-galactosidase activities of yeast transformed with plasmids containing fusions of lacZ to the upstream regions of SDH1 and SDH1b [3].

Associations of SDH1 with chemical compounds

• The membrane extrinsic domain, consisting of Sdh1p and Sdh2p, contains a covalent FAD cofactor and three iron-sulfur clusters [6].
• The sdh1 sdh1b disruptant showed a marked increase in succinate productivity of up to 1.9-fold along with a decrease in malate productivity relative to the wild-type strains under shaking conditions [7].

Other interactions of SDH1

• The yeast succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits, Sdh1p-Sdh4p, that couples the oxidation of succinate to the transfer of electrons to ubiquinone [8].

References