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PARL Deficiency in Mouse Causes Complex III Defects, Coenzyme Q Depletion, and Leigh-Like Syndrome
PARL deficiency in mouse causes Complex III defects, coenzyme Q depletion, and Leigh-like syndrome Marco Spinazzia,b,1, Enrico Radaellic, Katrien Horréa,b, Amaia M. Arranza,b, Natalia V. Gounkoa,b,d, Patrizia Agostinise, Teresa Mendes Maiaf,g,h, Francis Impensf,g,h, Vanessa Alexandra Moraisi, Guillermo Lopez-Lluchj,k, Lutgarde Serneelsa,b, Placido Navasj,k, and Bart De Stroopera,b,l,1 aVIB Center for Brain and Disease Research, 3000 Leuven, Belgium; bDepartment of Neurosciences, Katholieke Universiteit Leuven, 3000 Leuven, Belgium; cComparative Pathology Core, Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104-6051; dElectron Microscopy Platform, VIB Bio Imaging Core, 3000 Leuven, Belgium; eCell Death Research & Therapy Laboratory, Department for Cellular and Molecular Medicine, Katholieke Universiteit Leuven, 3000 Leuven, Belgium; fVIB Center for Medical Biotechnology, VIB, 9000 Ghent, Belgium; gVIB Proteomics Core, VIB, 9000 Ghent, Belgium; hDepartment for Biomolecular Medicine, Ghent University, 9000 Ghent, Belgium; iInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisbon, Portugal; jCentro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide-Consejo Superior de Investigaciones Científicas-Junta de Andalucía, 41013 Seville, Spain; kCentro de Investigaciones Biomédicas en Red de Enfermedades Raras, Instituto de Salud Carlos III, 28029 Madrid, Spain; and lUK Dementia Research Institute, University College London, WC1E 6BT London, United Kingdom Edited by Richard D. Palmiter, University of Washington, Seattle, WA, and approved November 21, 2018 (received for review July 11, 2018) The mitochondrial intramembrane rhomboid protease PARL has been proposed that PARL exerts proapoptotic effects via misprocessing implicated in diverse functions in vitro, but its physiological role in of the mitochondrial Diablo homolog (hereafter DIABLO) (10). -
UQCRFS1N Assembles Mitochondrial Respiratory Complex-III Into an Asymmetric 21-Subunit Dimer
Protein Cell 2018, 9(6):586–591 https://doi.org/10.1007/s13238-018-0515-x Protein & Cell LETTER TO THE EDITOR UQCRFS1N assembles mitochondrial respiratory complex-III into an asymmetric 21-subunit dimer Dear Editor, Although several structures have been solved with very high resolution, the full length N-terminal processed peptide (1– Mitochondrial respiratory chain consists of four multimeric 78 amino acids, UQCRFS1N) of the iron-sulfur Rieske pro- protein complexes, Complex I-IV (CI, NADH dehydroge- tein (UQCRFS1) subunit has not been assigned in all of nase; CII, succinate:ubiquinone oxidoreductase; CIII, cyto- these structures (Table 1). UQCRFS1N is the N-terminal chrome bc1 complex; and CIV, cytochrome c oxidase). Cell mitochondrial targeting sequence of UQCRFS1, and after its These four complexes transfer electrons from NADH or cleavage from the precursor, this small peptide remains & FADH to oxygen and pump protons from mitochondrial 2 bound to CIII with unknown functions. In this letter, we show matrix to intermembrane space, generating electrochemical that one UQCRFS1N links the two 10-subunit CIII protomers gradient across the inner membrane which is harnessed by together to form the intact CIII, which resultantly contains complex V to synthesize ATP, providing the majority of only 21 subunits rather than previously assumed 22 subunits energy acquired by living organisms. Respiratory chain Protein (Fig. 1A and 1B). complexes were reported to interact with each other to form Firstly, we rebuilt the high-resolution crystal structures of supercomplexes, even megacomplex (Guo et al., 2017). bovine CIII (PDB: 2A06) (Huang et al., 2005) and chicken However, despite decades of intensive research, many CIII (PDB:3TGU) (Hao et al., 2012). -
Roles of Mitochondrial Respiratory Complexes During Infection Pedro Escoll, Lucien Platon, Carmen Buchrieser
Roles of Mitochondrial Respiratory Complexes during Infection Pedro Escoll, Lucien Platon, Carmen Buchrieser To cite this version: Pedro Escoll, Lucien Platon, Carmen Buchrieser. Roles of Mitochondrial Respiratory Complexes during Infection. Immunometabolism, Hapres, 2019, Immunometabolism and Inflammation, 1, pp.e190011. 10.20900/immunometab20190011. pasteur-02593579 HAL Id: pasteur-02593579 https://hal-pasteur.archives-ouvertes.fr/pasteur-02593579 Submitted on 15 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License ij.hapres.com Review Roles of Mitochondrial Respiratory Complexes during Infection Pedro Escoll 1,2,*, Lucien Platon 1,2,3, Carmen Buchrieser 1,2,* 1 Institut Pasteur, Unité de Biologie des Bactéries Intracellulaires, 75015 Paris, France 2 CNRS-UMR 3525, 75015 Paris, France 3 Faculté des Sciences, Université de Montpellier, 34095 Montpellier, France * Correspondence: Pedro Escoll, Email: [email protected]; Tel.: +33-0-1-44-38-9540; Carmen Buchrieser, Email: [email protected]; Tel.: +33-0-1-45-68-8372. ABSTRACT Beyond oxidative phosphorylation (OXPHOS), mitochondria have also immune functions against infection, such as the regulation of cytokine production, the generation of metabolites with antimicrobial proprieties and the regulation of inflammasome-dependent cell death, which seem in turn to be regulated by the metabolic status of the organelle. -
Severe Respiratory Complex III Defect Prevents Liver Adaptation To
Severe respiratory complex III defect prevents liver adaptation to prolonged fasting Laura Kremer, Caroline L ’Hermitte-Stead, Pierre Lesimple, Mylène Gilleron, Sandrine Filaut, Claude Jardel, Tobias Haack, Tim Strom, Thomas Meitinger, Hatem Azzouz, et al. To cite this version: Laura Kremer, Caroline L ’Hermitte-Stead, Pierre Lesimple, Mylène Gilleron, Sandrine Filaut, et al.. Severe respiratory complex III defect prevents liver adaptation to prolonged fasting. Journal of Hepatology, Elsevier, 2016, 65 (2), pp.377-85. 10.1016/j.jhep.2016.04.017. inserm-01321215 HAL Id: inserm-01321215 https://www.hal.inserm.fr/inserm-01321215 Submitted on 25 May 2016 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. 1 Severe respiratory complex III defect prevents liver adaptation to prolonged fasting Laura S Kremer1,2, Caroline L’hermitte- Stead3,4,5, Pierre Lesimple3,4,5, Mylène Gilleron3,4,5,6, Sandrine Filaut6, Claude Jardel3,4,5,6, Tobias B Haack1,2, Tim M Strom1,2, Thomas Meitinger1,2, Hatem Azzouz7, Neji Tebib7, Hélène Ogier de Baulny8, Guy Touati9, Holger Prokisch1, -
Clinical and Molecular Characterization of Three Patients
Mahjoub et al. BMC Medical Genetics (2019) 20:167 https://doi.org/10.1186/s12881-019-0893-9 CASE REPORT Open Access Clinical and molecular characterization of three patients with Hepatocerebral form of mitochondrial DNA depletion syndrome: a case series Ghazale Mahjoub1, Parham Habibzadeh1,2, Hassan Dastsooz1,3, Malihe Mirzaei1, Arghavan Kavosi1, Laila Jamali1, Haniyeh Javanmardi2, Pegah Katibeh4, Mohammad Ali Faghihi1,5 and Seyed Alireza Dastgheib6* Abstract Background: Mitochondrial DNA depletion syndromes (MDS) are clinically and phenotypically heterogeneous disorders resulting from nuclear gene mutations. The affected individuals represent a notable reduction in mitochondrial DNA (mtDNA) content, which leads to malfunction of the components of the respiratory chain. MDS is classified according to the type of affected tissue; the most common type is hepatocerebral form, which is attributed to mutations in nuclear genes such as DGUOK and MPV17. These two genes encode mitochondrial proteins and play major roles in mtDNA synthesis. Case presentation: In this investigation patients in three families affected by hepatocerebral form of MDS who were initially diagnosed with tyrosinemia underwent full clinical evaluation. Furthermore, the causative mutations were identified using next generation sequencing and were subsequently validated using sanger sequencing. The effect of the mutations on the gene expression was also studied using real-time PCR. A pathogenic heterozygous frameshift deletion mutation in DGUOK gene was identified in parents of two affected patients (c.706–707 + 2 del: p.k236 fs) presenting with jaundice, impaired fetal growth, low-birth weight, and failure to thrive who died at the age of 3 and 6 months in family I. Moreover, a novel splice site mutation in MPV17 gene (c.461 + 1G > C) was identified in a patient with jaundice, muscle weakness, and failure to thrive who died due to hepatic failure at the age of 4 months. -
Introduction Results Patients and Methods
Célia Nogueira 1, José Barros 2, Maria José Sá 3, Luísa Azevedo 4, Filippo M. Santorelli 5, Laura Vilarinho 1 1National Institute of Health, Genetics Department, INSA, Oporto, Portugal; 2Neurology Unit, Hospital S. António, Oporto, Portugal; 3Neurology Unit, Hospital S. João, Oporto, Portugal; 4IPATIMUP, Population Genetics, Oporto University, Oporto, Portugal; 5Fundazione Stella Maris, Molecular Medicine & Neurogenetics, IRCCS, Pisa, Italy. INTRODUCTION RESULTS Defects of mitochondrial complex III (CIII) are a relatively rare cause of We had first detected a biochemically deficient enzyme activity in the mitochondrial dysfunction. CIII or ubiquinol-cytochrome c reductase is family, we had analyzed all structural genes part of CIII as well as the third component of the mitochondrial respiratory chain and catalyzes BCS1L. Only the recent description of mutations in TTC19 raised high the electrons transfer from reduced coenzyme Q to cytochrome c and is the suspect of a similar condition in the present family. The novel composed of 11 subunits ; one encoded by mitochondrial DNA (MT -CYB ) TTC 19 mutation p.A321 AfsX 8 (c .962 _967 delTGGC), identified in this and the remaining by nuclear genes [1]. BCS1L gene is a CIII assembly family, was homozygous in the four patients, heterozygous in their factor. Mutations in MT-CYB and BCS1L genes account for the vast parents and in two healthy relatives, and it was absent in ethnically- majority of mutations leading to CIII deficiency, and are associated with matched controls (Figure 2). a wide range of neuromuscular disorders [2]. The human tetratricopeptide 19 (TTC19), encodes a poorly understood A B member of tetratricopeptide repeat domain 19 located on chromosome 17 and appears to be involved in the correct assembly of CIII. -
Imaging Patterns Characterizing Mitochondrial Leukodystrophies
Published April 1, 2021 as 10.3174/ajnr.A7097 ORIGINAL RESEARCH PEDIATRICS Imaging Patterns Characterizing Mitochondrial Leukodystrophies S.D. Roosendaal, T. van de Brug, C.A.P.F. Alves, S. Blaser, A. Vanderver, N.I. Wolf, and M.S. van der Knaap ABSTRACT BACKGROUND AND PURPOSE: Achieving a specific diagnosis in leukodystrophies is often difficult due to clinical and genetic heter- ogeneity. Mitochondrial defects cause 5%–10% of leukodystrophies. Our objective was to define MR imaging features commonly shared by mitochondrial leukodystrophies and to distinguish MR imaging patterns related to specific genetic defects. MATERIALS AND METHODS: One hundred thirty-two patients with a mitochondrial leukodystrophy with known genetic defects were identified in the data base of the Amsterdam Leukodystrophy Center. Numerous anatomic structures were systematically assessed on brain MR imaging. Additionally, lesion characteristics were scored. Statistical group analysis was performed for 57 MR imaging features by hierarchic testing on clustered genetic subgroups. RESULTS: MR imaging features indicative of mitochondrial disease that were frequently found included white matter rarefaction (n ¼ 50 patients), well-delineated cysts (n ¼ 20 patients), T2 hyperintensity of the middle blade of the corpus callosum (n ¼ 85 patients), and symmetric abnormalities in deep gray matter structures (n ¼ 42 patients). Several disorders or clusters of disorders had characteristic features. The combination of T2 hyperintensity in the brain stem, middle cerebellar peduncles, and thalami was associated with complex 2 deficiency. Predominantly periventricular localization of T2 hyperintensities and cystic lesions with a dis- tinct border was associated with defects in complexes 3 and 4. T2-hyperintense signal of the cerebellar cortex was specifically associated with variants in the gene NUBPL. -
A Novel Mutation in TTC19 Associated with Isolated Complex III Deficiency
ORIGINAL RESEARCH ARTICLE published: 14 November 2014 doi: 10.3389/fgene.2014.00397 A novel mutation inTTC19 associated with isolated complex III deficiency, cerebellar hypoplasia, and bilateral basal ganglia lesions Laura Melchionda1, Nadirah S. Damseh 2 , Bassam Y. Abu Libdeh 2 , Alessia Nasca 1, Orly Elpeleg 3 , Alice Zanolini 1 and Daniele Ghezzi 1* 1 Unit of Molecular Neurogenetics, Foundation IRCCS Istituto Neurologico Carlo Besta, Milan, Italy 2 Genetic Unit, Al-Makassed Islamic Charitable Hospital, Jerusalem, Israel 3 Monique and Jacques Roboh Department of Genetic Research, Hadassah – Hebrew University Medical Center, Jerusalem, Israel Edited by: Isolated complex III (cIII) deficiency is a rare biochemical finding in mitochondrial disor- Claudia Zanna, University of Bologna, ders, mainly associated with mutations in mitochondrial DNA MTCYB gene, encoding Italy cytochrome b, or in assembly factor genes (BCS1L,TTC19, UQCC2, and LYRM7), whereas Reviewed by: mutations in nuclear genes encoding cIII structural subunits are extremely infrequent. We Erika Fernandez-Vizarra, Medical Research Council, UK report here a patient, a 9 year old female born from first cousin related parents, with Paldeep Atwal, Baylor College of normal development till 18 months when she showed unsteady gait with frequent falling Medicine, USA down, cognitive, and speech worsening. Her course deteriorated progressively. Brain Célia Nogueira, Instituto Nacional de Saúde-Porto, Portugal MRI showed cerebellar vermis hypoplasia and bilateral lentiform nucleus high signal lesions. Now she is bed ridden with tetraparesis and severely impaired cognitive and *Correspondence: Daniele Ghezzi, Unit of Molecular language functions. Biochemical analysis revealed isolated cIII deficiency in muscle, and Neurogenetics, Foundation IRCCS impaired respiration in fibroblasts. -
Mrna-Binding Protein Tristetraprolin Is Essential for Cardiac Response To
mRNA-binding protein tristetraprolin is essential for PNAS PLUS cardiac response to iron deficiency by regulating mitochondrial function Tatsuya Satoa,1, Hsiang-Chun Changa,1, Marina Bayevaa, Jason S. Shapiroa, Lucia Ramos-Alonsob, Hidemichi Kouzua, Xinghang Jianga, Ting Liua, Sumeyye Yara, Konrad T. Sawickia, Chunlei Chena, María Teresa Martínez-Pastorc, Deborah J. Stumpod, Paul T. Schumackere, Perry J. Blacksheard, Issam Ben-Sahraf, Sergi Puigb, and Hossein Ardehalia,2 aFeinberg Cardiovascular Research Institute, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611; bDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas, 46980 Paterna, Valencia, Spain; cDepartamento de Bioquímica y Biología Molecular, Universitat de València, 46100 Burjassot, Valencia, Spain; dSignal Transduction Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709; eDepartment of Pediatrics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611; and fDepartment of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611 Edited by J. G. Seidman, Harvard Medical School, Boston, MA, and approved May 23, 2018 (received for review March 23, 2018) Cells respond to iron deficiency by activating iron-regulatory electron transport chain (ETC) (11). However, energy pro- proteins to increase cellular iron uptake and availability. However, duction by oxidative phosphorylation in mitochondria is non- it is not clear how cells adapt to conditions when cellular iron essential for survival, at least in the short term, as demonstrated uptake does not fully match iron demand. Here, we show that the by a switch to anaerobic respiration and heavy reliance on gly- mRNA-binding protein tristetraprolin (TTP) is induced by iron colysis in muscle during vigorous exercise, when oxygen demand deficiency and degrades mRNAs of mitochondrial Fe/S-cluster- outmatches its supply (12). -
Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces Cerevisiae
life Review Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces cerevisiae Leticia V. R. Franco 1,2,* , Luca Bremner 1 and Mario H. Barros 2 1 Department of Biological Sciences, Columbia University, New York, NY 10027, USA; [email protected] 2 Department of Microbiology,Institute of Biomedical Sciences, Universidade de Sao Paulo, Sao Paulo 05508-900, Brazil; [email protected] * Correspondence: [email protected] Received: 27 October 2020; Accepted: 19 November 2020; Published: 23 November 2020 Abstract: The ease with which the unicellular yeast Saccharomyces cerevisiae can be manipulated genetically and biochemically has established this organism as a good model for the study of human mitochondrial diseases. The combined use of biochemical and molecular genetic tools has been instrumental in elucidating the functions of numerous yeast nuclear gene products with human homologs that affect a large number of metabolic and biological processes, including those housed in mitochondria. These include structural and catalytic subunits of enzymes and protein factors that impinge on the biogenesis of the respiratory chain. This article will review what is currently known about the genetics and clinical phenotypes of mitochondrial diseases of the respiratory chain and ATP synthase, with special emphasis on the contribution of information gained from pet mutants with mutations in nuclear genes that impair mitochondrial respiration. Our intent is to provide the yeast mitochondrial specialist with basic knowledge of human mitochondrial pathologies and the human specialist with information on how genes that directly and indirectly affect respiration were identified and characterized in yeast. Keywords: mitochondrial diseases; respiratory chain; yeast; Saccharomyces cerevisiae; pet mutants 1. -
Transcriptomic and Proteomic Landscape of Mitochondrial
TOOLS AND RESOURCES Transcriptomic and proteomic landscape of mitochondrial dysfunction reveals secondary coenzyme Q deficiency in mammals Inge Ku¨ hl1,2†*, Maria Miranda1†, Ilian Atanassov3, Irina Kuznetsova4,5, Yvonne Hinze3, Arnaud Mourier6, Aleksandra Filipovska4,5, Nils-Go¨ ran Larsson1,7* 1Department of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany; 2Department of Cell Biology, Institute of Integrative Biology of the Cell (I2BC) UMR9198, CEA, CNRS, Univ. Paris-Sud, Universite´ Paris-Saclay, Gif- sur-Yvette, France; 3Proteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany; 4Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia; 5School of Molecular Sciences, The University of Western Australia, Crawley, Australia; 6The Centre National de la Recherche Scientifique, Institut de Biochimie et Ge´ne´tique Cellulaires, Universite´ de Bordeaux, Bordeaux, France; 7Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden Abstract Dysfunction of the oxidative phosphorylation (OXPHOS) system is a major cause of human disease and the cellular consequences are highly complex. Here, we present comparative *For correspondence: analyses of mitochondrial proteomes, cellular transcriptomes and targeted metabolomics of five [email protected] knockout mouse strains deficient in essential factors required for mitochondrial DNA gene (IKu¨ ); expression, leading to OXPHOS dysfunction. Moreover, -
Thesis Reference
Thesis C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization DESMURS-ROUSSEAU, Marjorie Abstract Cette thèse a permis d'identifier C11orf83, désormais appelé UQCC3, comme étant une protéine mitochondriale ancrée dans la membrane interne. Nous avons constaté l'implication de C11orf83 dans l'assemblage du complexe III de la chaîne respiratoire via la stabilisation du complexe intermédiaire MT-CYB/UQCRB/UQCRQ. Nous avons également prouvé que C11orf83 était associée avec le dimère de complexe III et était détectée dans le supercomplexe III2/IV. Son absence induit une baisse significative de ce supercomplexe et du respirasome (I/III2/IV). La capacité de C11orf83 de lier les cardiolipines, connues pour être impliquées dans la formation et la stabilisation de ces supercomplexes, pourrait expliquer ces résultats. Ainsi, ce travail de thèse en lien avec une récente étude clinique mettant en évidence une déficience du complexe III chez un patient atteint d'une mutation du gène C11orf83 (Wanschers et al., 2014) permet d'améliorer les connaissances sur l'assemblage du complexe III et la compréhension d'une maladie mitochondriale. Reference DESMURS-ROUSSEAU, Marjorie. C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization. Thèse de doctorat : Univ. Genève, 2015, no. Sc. 4857 DOI : 10.13097/archive-ouverte/unige:108015 URN : urn:nbn:ch:unige-1080158 Available at: http://archive-ouverte.unige.ch/unige:108015 Disclaimer: layout of this document may differ from the published version. 1 / 1 UNIVERSITÉ DE GENÈVE Département de Biologie Cellulaire FACULTÉ DES SCIENCES Professeur Jean-Claude Martinou Département de Science des Protéines Humaines FACULTÉ DE MEDECINE Professeur Amos Bairoch C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization.