ArticleThe Journal of biological chemistry2012
Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025Review
- The cytochromeLife science alliance · 2023Article
- Systematic Assessment of Protein C-Termini Mutated in Human Disorders.Biomolecules · 2023Article
- Succinate dehydrogenase complex subunit C: Role in cellular physiology and disease.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies ofLife (Basel, Switzerland) · 2020Review
- Blackout in the powerhouse: clinical phenotypes associated with defects in the assembly of OXPHOS complexes and the mitoribosome.The Biochemical journal · 2020Review
- The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Respiratory supercomplexes act as a platform for complex III-mediated maturation of human mitochondrial complexes I and IV.The EMBO journal · 2020Article
- The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019Review
- Unique genetic basis of the distinct antibiotic potency of high acetic acid production in the probiotic yeastGenome research · 2019Article
- Complete Native Stable Isotope Labeling by Amino Acids of Saccharomyces cerevisiae for Global Proteomic Analysis.Analytical chemistry · 2018Article
- Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.Essays in biochemistry · 2018Review
- Crystal structure of an assembly intermediate of respiratory Complex II.Nature communications · 2018Article
- Biochemical, Molecular, and Clinical Characterization of Succinate Dehydrogenase Subunit A Variants of Unknown Significance.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017Article
- Structural and biochemical analyses reveal insights into covalent flavinylation of theThe Journal of biological chemistry · 2017Article
- Article
- SLC25 Family Member Genetic Interactions Identify a Role forG3 (Bethesda, Md.) · 2017Article
- Analysis of transcriptional profiles of Saccharomyces cerevisiae exposed to bisphenol A.Current genetics · 2017Article
- Article
- Disease-Causing SDHAF1 Mutations Impair Transfer of Fe-S Clusters to SDHB.Cell metabolism · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
backgroundSuccinate dehydrogenase (SDH) requires a covalent addition of FAD for catalytic function.
resultsMutational analyses of Sdh1 implicate C-terminal region Arg residues involvement in covalent flavinylation and SDH assembly.
conclusionSDH assembly is dependent on FAD binding to Sdh1 but not covalent binding. SIGNIFICANCE: These results document the basis for the SDH deficiency and pathology seen with mutations in human Sdh1. The enzymatic function of succinate dehydrogenase (SDH) is dependent on covalent attachment of FAD on the ~70-kDa flavoprotein subunit Sdh1. We show presently that flavinylation of the Sdh1 subunit of succinate dehydrogenase is dependent on a set of two spatially close C-terminal arginine residues that are distant from the FAD binding site. Mutation of Arg(582) in yeast Sdh1 precludes flavinylation as well as assembly of the tetrameric enzyme complex. Mutation of Arg(638) compromises SDH function only when present in combination with a Cys(630) substitution. Mutations of either Arg(582) or Arg(638)/Cys(630) do not markedly destabilize the Sdh1 polypeptide; however, the steady-state level of Sdh5 is markedly attenuated in the Sdh1 mutant cells. With each mutant Sdh1, second-site Sdh1 suppressor mutations were recovered in Sdh1 permitting flavinylation, stabilization of Sdh5 and SDH tetramer assembly. SDH assembly appears to require FAD binding but not necessarily covalent FAD attachment. The Arg residues may be important not only for Sdh5 association but also in the recruitment and/or guidance of FAD and or succinate to the substrate site for the flavinylation reaction. The impaired assembly of SDH with the C-terminal Sdh1 mutants suggests that FAD binding is important to stabilize the Sdh1 conformation enabling association with Sdh2 and the membrane anchor subunits.
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