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- W2070307065 abstract "A mutation of the mitochondrial protein SDH assembly factor 2 (AF2) has been linked to hereditary paraganglioma in humans (Hao et al.(2009), Science 325,1139-42). These authors showed that AF2 is required for flavinylation of the succinate dehydrogenase flavoprotein (SDHA) in human cells or yeast, and that yeast SDHA heterogenously expressed in E. coli is flavinated only if yeast AF2 is coexpressed. We have extended these observations to the human protein: hSDHA is flavinated in E. coli only if coexpressed with human AF2. Flavinylation does not occur when purified recombinant hSDHA and AF2 are mixed with FAD in the presence or absence of succinate, fumarate, and MgATP, so some other factor provided by E. coli is required. We will report results fractionating E. coli cell lysate to determine the factors required and elucidate the role of AF2 in flavinylation. The E. coli protein YgfY is a distant homolog of mitochondrial AF2, and E. coli has SDH, the flavoprotein of which is very similar to that of mitochondrial SDH. We show here that a strain of E. coli with YgfY deleted is unable to grow with succinate as carbon source or to accumulate flavinylated SDH flavoprotein in its membranes. These observations are consistent with but do not prove a role for YgfY in maturation of SDH flavoprotein." @default.
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- W2070307065 date "2013-01-01" @default.
- W2070307065 modified "2023-09-26" @default.
- W2070307065 title "The Role of SDH Assembly Factor 2 and YgfY in Flavinylation of Succinate Dehydrogenase Flavoprotein" @default.
- W2070307065 doi "https://doi.org/10.1016/j.bpj.2012.11.296" @default.
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