Tissue Specificity of a Human Mitochondrial Disease

Crooks, Daniel R.; Jeong, Suh Young; Tong, Wing H.; Ghosh, Manik C.; Olivierre, Hayden; Haller, Ronald G.; Rouault, Tracey A.

doi:10.1074/jbc.m112.418889

Cited by 34 publications

(23 citation statements)

References 48 publications

(57 reference statements)

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“…The point mutation was an intronic G to C transversion (7044G-C) in the ISCU gene, which strengthened a weak splice acceptor site and resulted in the retention of a 100 base pair (bp) fragment of intron 5 in the mature mRNA. The aberrantly spliced ISCU mRNA encoded the wrong C-terminal sequence, which ends with a premature stop codon, leading to translation of a truncated protein with a markedly reduced half-life [230]. Given the role of ISCU as the primary scaffold for Fe-S cluster biogenesis, the mutation leads to adverse effects on Fe-S protein biogenesis and intracellular iron homeostasis.…”

Section: Iscu Myopathy Also Known As Hereditary Myopathy With Lacticmentioning

confidence: 99%

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Maio

Rouault

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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175

178

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Iron-sulfur (Fe-S) clusters are ancient, ubiquitous cofactors composed of iron and inorganic sulfur. The combination of the chemical reactivity of iron and sulfur, together with many variations of cluster composition, oxidation states and protein environments, enables Fe-S clusters to participate in numerous biological processes. Fe-S clusters are essential to redox catalysis in nitrogen fixation, mitochondrial respiration and photosynthesis, to regulatory sensing in key metabolic pathways (i. e. cellular iron homeostasis and oxidative stress response), and to the replication and maintenance of the nuclear genome. Fe-S cluster biogenesis is a multistep process that involves a complex sequence of catalyzed protein- protein interactions and coupled conformational changes between the components of several dedicated multimeric complexes. Intensive studies of the assembly process have clarified key points in the biogenesis of Fe-S proteins. However several critical questions still remain, such as: what is the role of frataxin? Why do some defects of Fe-S cluster biogenesis cause mitochondrial iron overload? How are specific Fe-S recipient proteins recognized in the process of Fe-S transfer? This review focuses on the basic steps of Fe-S cluster biogenesis, drawing attention to recent advances achieved on the identification of molecular features that guide selection of specific subsets of nascent Fe-S recipients by the cochaperone HSC20. Additionally, it outlines the distinctive phenotypes of human diseases due to mutations in the components of the basic pathway.

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Section: Iscu Myopathy Also Known As Hereditary Myopathy With Lacticmentioning

confidence: 99%

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Maio

Rouault

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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175

178

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“…Similar to FRDA, the IM phenotype is inherited in an autosomal recessive pattern. IM is caused by a splicing defect during ISCU post-transcriptional processing that leads to defective ISCU protein 182,183 . Loss of ISCU leads to lower ISC activity and a resulting deficiency of essential Fe-S proteins, including succinate dehydrogenase and aconitase of the citric acid cycle 184 .…”

Section: Fe-s Clustersmentioning

confidence: 99%

Synthesis, delivery and regulation of eukaryotic heme and Fe–S cluster cofactors

Barupala

Dzul

Riggs-Gelasco

et al. 2016

Archives of Biochemistry and Biophysics

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In humans, the bulk of iron in the body (over 75%) is directed towards heme- or Fe-S cluster cofactor synthesis, and the complex, highly regulated pathways in place to accomplish biosynthesis have evolved to safely assemble and load these cofactors into apoprotein partners. In eukaryotes, heme biosynthesis is both initiated and finalized within the mitochondria, while cellular Fe-S cluster assembly is controlled by correlated pathways both within the mitochondria and within the cytosol. Iron plays a vital role in a wide array of metabolic processes and defects in iron cofactor assembly leads to human diseases. This review describes progress towards our molecular-level understanding of cellular heme and Fe-S cluster biosynthesis, focusing on the regulation and mechanistic details that are essential for understanding human disorders related to the breakdown in these essential pathways.

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“…Yeast depleted of ISU components or the Fe-S targeting factors Grx5, ISA components and Nfu1 are impaired in SDH activity (Jensen and Culotta, 2000, Rodriguez-Manzaneque et al, 2002, Muhlenhoff et al, 2011). Mutations in human orthologs of Isd11, Isu1, Iba57 or Nfu1 (Crooks et al, 2012, Hall et al, 1993, Lim et al, 2013, Navarro-Sastre et al, 2011, Cameron et al, 2011, Ferrer-Cortes et al, 2013, Ajit Bolar et al, 2013) or RNAi depletion of Isa1, or Isa2 lead to compromised SDH function (Sheftel et al, 2012) (Figure 2). …”

Section: Sdh2—the Electron Wirementioning

confidence: 99%

Protein-mediated assembly of succinate dehydrogenase and its cofactors

Vranken¹,

Winge

et al. 2014

Critical Reviews in Biochemistry and Molecular Biology

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Succinate dehydrogenase (or Complex II; SDH) is a heterotetrameric protein complex that links the tribarboxylic acid cycle with the electron transport chain. SDH is composed of four nuclear-encoded subunits that must translocate independently to the mitochondria and assemble into a mature protein complex embedded in the inner mitochondrial membrane. Recently, it has become clear that failure to assemble functional SDH complexes can result in cancer and neurodegenerative syndromes. The effort to thoroughly elucidate the SDH assembly pathway has resulted in the discovery of four subunit-specific assembly factors that aid in the maturation of individual subunits and support the assembly of the intact complex. This review will focus on these assembly factors and assess the contribution of each factor to the assembly of SDH. Finally, we propose a model of the SDH assembly pathway that incorporates all extant data.

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Tissue Specificity of a Human Mitochondrial Disease

Cited by 34 publications

References 48 publications

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Synthesis, delivery and regulation of eukaryotic heme and Fe–S cluster cofactors

Protein-mediated assembly of succinate dehydrogenase and its cofactors

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