UQCRFS1 Antibody

Total Page：16

File Type：pdf, Size：1020Kb

Efficient Professional Protein and Antibody Platforms UQCRFS1 Antibody Basic information: Catalog No.: UPA63625 Source: Rabbit Size: 50ul/100ul Clonality: Monoclonal Concentration: 1mg/ml Isotype: Rabbit IgG Purification: Protein A affinity purified Useful Information: WB:1:500-1:2000 ICC:1:500-1:2000 Applications: IHC:1:50-1:200 FC:1:50-1:100 FC:1:10-1:50 Reactivity: Human, Mouse, Rat Specificity: This antibody recognizes UQCRFS1 protein. Immunogen: Recombinant protein within human UQCRFS1 aa 100 to the C-terminus. Cytochrome b-c1 complex subunit Rieske, mitochondrial: Component of the mitochondrial ubiquinol-cytochrome c reductase complex dimer (complex Description: III dimer), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. Incorporation of UQCRFS1 is the penul- timate step in complex III assembly. Uniprot: P47985(Human) Q9CR68(Mouse) P20788(Rat) BiowMW: 21 kDa Buffer: 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide. Storage: Store at 4°C short term and -20°C long term. Avoid freeze-thaw cycles. Note: For research use only, not for use in diagnostic procedure. Data: Western blot analysis of UQCRFS1 on different lysates using anti-UQCRFS1 antibody at 1/1,000 dilution. Positive control: Lane 1: A549 Lane 2: 293 Lane 3: Mouse kidney Gene Universal Technology Co. Ltd www.universalbiol.com Tel: 0550-3121009 E-mail: [email protected] Efficient Professional Protein and Antibody Platforms ICC staining UQCRFS1 in 293T cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS. ICC staining UQCRFS1 in LOVO cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS. ICC staining UQCRFS1 in SiHa cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS. Gene Universal Technology Co. Ltd www.universalbiol.com Tel: 0550-3121009 E-mail: [email protected] .

Copy Link

Recommended publications

The Landscape of Genomic Imprinting Across Diverse Adult Human Tissues
Downloaded from genome.cshlp.org on September 30, 2021 - Published by Cold Spring Harbor Laboratory Press Research The landscape of genomic imprinting across diverse adult human tissues Yael Baran,1 Meena Subramaniam,2 Anne Biton,2 Taru Tukiainen,3,4 Emily K. Tsang,5,6 Manuel A. Rivas,7 Matti Pirinen,8 Maria Gutierrez-Arcelus,9 Kevin S. Smith,5,10 Kim R. Kukurba,5,10 Rui Zhang,10 Celeste Eng,2 Dara G. Torgerson,2 Cydney Urbanek,11 the GTEx Consortium, Jin Billy Li,10 Jose R. Rodriguez-Santana,12 Esteban G. Burchard,2,13 Max A. Seibold,11,14,15 Daniel G. MacArthur,3,4,16 Stephen B. Montgomery,5,10 Noah A. Zaitlen,2,19 and Tuuli Lappalainen17,18,19 1The Blavatnik School of Computer Science, Tel-Aviv University, Tel Aviv 69978, Israel; 2Department of Medicine, University of California San Francisco, San Francisco, California 94158, USA; 3Analytic and Translational Genetics Unit, Massachusetts General Hospital, Boston, Massachusetts 02114, USA; 4Program in Medical and Population Genetics, Broad Institute of Harvard and MIT, Cambridge, Massachusetts 02142, USA; 5Department of Pathology, Stanford University, Stanford, California 94305, USA; 6Biomedical Informatics Program, Stanford University, Stanford, California 94305, USA; 7Wellcome Trust Center for Human Genetics, Nuffield Department of Clinical Medicine, University of Oxford, Oxford, OX3 7BN, United Kingdom; 8Institute for Molecular Medicine Finland, University of Helsinki, 00014 Helsinki, Finland; 9Department of Genetic Medicine and Development, University of Geneva, 1211 Geneva, Switzerland;
[Show full text]
NDUFAB1 Protects Heart by Coordinating Mitochondrial Respiratory Complex
bioRxiv preprint doi: https://doi.org/10.1101/302281; this version posted April 16, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. NDUFAB1 Protects Heart by Coordinating Mitochondrial Respiratory Complex and Supercomplex Assembly Running title: Hou et al. Cardiac Protection by NDUFAB1 Tingting Hou 1; Rufeng Zhang 1; Chongshu Jian 1; Wanqiu Ding 1; Yanru Wang 1; Qi Ma 1; Xinli Hu 1; Heping Cheng 1,†; Xianhua Wang 1,† 1State Key Laboratory of Membrane Biology, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking-Tsinghua Center for Life Sciences, Institute of Molecular Medicine, Peking University, China. † Corresponding author. Xianhua Wang Tel: 86-10-62754605 Email: [email protected] Heping Cheng Tel: 86-10-62765957 Email: [email protected] bioRxiv preprint doi: https://doi.org/10.1101/302281; this version posted April 16, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract The impairment of mitochondrial bioenergetics, often coupled with exaggerated reactive oxygen species (ROS) production, is emerging as a common mechanism in diseases of organs with a high demand for energy, such as the heart. Building a more robust cellular powerhouse holds promise for protecting these organs in stressful conditions. Here, we demonstrate that NDUFAB1 (NADH:ubiquinone oxidoreductase subunit AB1), acts as a powerful cardio-protector by enhancing mitochondrial energy biogenesis. In particular, NDUFAB1 coordinates the assembly of respiratory complexes I, II, and III and supercomplexes, conferring greater capacity and efficiency of mitochondrial energy metabolism.
[Show full text]
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).
[Show full text]
The Human Genome Project
TO KNOW OURSELVES ❖ THE U.S. DEPARTMENT OF ENERGY AND THE HUMAN GENOME PROJECT JULY 1996 TO KNOW OURSELVES ❖ THE U.S. DEPARTMENT OF ENERGY AND THE HUMAN GENOME PROJECT JULY 1996 Contents FOREWORD . 2 THE GENOME PROJECT—WHY THE DOE? . 4 A bold but logical step INTRODUCING THE HUMAN GENOME . 6 The recipe for life Some definitions . 6 A plan of action . 8 EXPLORING THE GENOMIC LANDSCAPE . 10 Mapping the terrain Two giant steps: Chromosomes 16 and 19 . 12 Getting down to details: Sequencing the genome . 16 Shotguns and transposons . 20 How good is good enough? . 26 Sidebar: Tools of the Trade . 17 Sidebar: The Mighty Mouse . 24 BEYOND BIOLOGY . 27 Instrumentation and informatics Smaller is better—And other developments . 27 Dealing with the data . 30 ETHICAL, LEGAL, AND SOCIAL IMPLICATIONS . 32 An essential dimension of genome research Foreword T THE END OF THE ROAD in Little has been rapid, and it is now generally agreed Cottonwood Canyon, near Salt that this international project will produce Lake City, Alta is a place of the complete sequence of the human genome near-mythic renown among by the year 2005. A skiers. In time it may well And what is more important, the value assume similar status among molecular of the project also appears beyond doubt. geneticists. In December 1984, a conference Genome research is revolutionizing biology there, co-sponsored by the U.S. Department and biotechnology, and providing a vital of Energy, pondered a single question: Does thrust to the increasingly broad scope of the modern DNA research offer a way of detect- biological sciences.
[Show full text]
UQCRC2 Antibody
Efficient Professional Protein and Antibody Platforms UQCRC2 Antibody Basic information: Catalog No.: UPA60311 Source: Rabbit Size: 50ul/100ul Clonality: Polyclonal Concentration: 1mg/ml Isotype: Rabbit IgG Purification: Protein affinity purified. Useful Information: WB:1:1000-2000 ICC:1:50-1:200 Applications: IHC:1:50-1:200 FC:1:50-1:100 Reactivity: Human, Mouse, Rat Specificity: This antibody recognizes UQCRC2 protein. Immunogen: Recombinant protein within human UQCRC2 aa 100-350. Cytochrome c is a well characterized, mobile electron transport protein that is essential to energy conversion in all aerobic organisms. Cytochrome b as- sociates with cytochrome c subunit 1 and the Rieske protein to form com- plex III (also designated cytochrome bc1 complex), which is involved in cel- lular respiration. Ubiquinol cytochrome c reductase (UQCRFS1), also re- ferred to as Rieske iron-sulfur protein, represents an important subunit of Description: complex III of the mitochondrial respiratory chain that transfers electrons from ubiquinol to cytochrome c. The UQCRFS1 complex is made up of 3 res- piratory subunits (cytochrome b, cytochrome c1, Rieske protein), 2 core proteins, and 6 low-molecular weight proteins. Ubiquinol cytochrome-c re- ductase complex core protein 2 (UQCRC2) represents one of the core pro- teins of UQCRFS1, and it is required for the assembly of the complex. Uniprot: P22695(Human) Q9DB77(Mouse) P32551(Rat) BiowMW: 48 kDa Buffer: 1*TBS (pH7.4), 0.5%BSA, 50%Glycerol. Preservative: 0.05% Sodium Azide. Storage: Store at 4°C short term and -20°C long term. Avoid freeze-thaw cycles. Note: For research use only, not for use in diagnostic procedure.
[Show full text]
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).
[Show full text]
Datasheet Blank Template
SAN TA C RUZ BI OTEC HNOL OG Y, INC . UQCRC2 (H-135): sc-292924 BACKGROUND RECOMMENDED SECONDARY REAGENTS Cytochrome c is a well characterized, mobile electron transport protein that To ensure optimal results, the following support (secondary) reagents are is essential to energy conversion in all aerobic organisms. Cytochrome b asso - recommended: 1) Western Blotting: use goat anti-rabbit IgG-HRP: sc-2004 ciates with cytochrome c subunit 1 and the Rieske protein to form complex III (dilution range: 1:2000-1:100,000) or Cruz Marker™ compatible goat anti- (also designated cytochrome bc1 complex), which is involved in cellular res - rabbit IgG-HRP: sc-2030 (dilution range: 1:2000-1:5000), Cruz Marker™ piration. Ubiquinol cytochrome c reductase (UQCRFS1), also referred to as Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: Rieske iron-sulfur protein, represents an important subunit of complex III of sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunoprecip- the mitochondrial respiratory chain that transfers electrons from ubiquinol to itation: use Protein A/G PLUS-Agarose: sc-2003 (0.5 ml agarose/2.0 ml). cytochrome c. The UQCRFS1 complex is made up of three respiratory sub - 3) Immunofluorescence: use goat anti-rabbit IgG-FITC: sc-2012 (dilution units (cytochrome b, cytochrome c1, Rieske protein), two core proteins, and range: 1:100-1:400) or goat anti-rabbit IgG-TR: sc-2780 (dilution range: six low-molecular weight proteins. Ubiquinol cytochrome-c reductase com plex 1:100-1:400) with UltraCruz™ Mounting Medium: sc-24941. core protein 2 (UQCRC2) represents one of the core proteins of UQCRFS1, and it is required for the assembly of the complex.
[Show full text]
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.
[Show full text]
Structure, Sequence and Location of the UQCRFS1 Gene for the Human Rieske Fe-S Protein
Gene, 155 (1995) 207-211 © 1995 Elsevier Science B.V. All rights reserved. 0378-1119/95/$09.50 207 GENE 08472 Structure, sequence and location of the UQCRFS1 gene for the human Rieske Fe-S protein (Recombinant DNA; nuclear gene; respiratory chain; electron transport; mitochondrial protein; myopathy; nucleotide sequencing; chromosome 19q12; Homo sapiens) Len A. Pennacchio a, Anne Bergmann a, Atsushi Fukushima b, Kousaku Okubo b, Arash Salemi a and Gregory G. Lennon a aHuman Genome Center, Biology & Biotechnology Research Program, L-452, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA; and blnstitute for Molecular and Cellular Biology, Osaka University, I-3 Yamada-oka, Suita, Osaka 565, Japan Received by J.A. Engler: 15 June 1994; Revised/Accepted: 12 August/15 August 1994; Received at publishers: 29 September 1994 SUMMARY We have identified and studied the chromosomal location of the human Rieske Fe-S protein-encoding gene UQCRFS1. Mapping by hybridization to a panel of monochromosomal hybrid cell lines indicated that a UQCRFS1 partial cDNA was derived from either chromosome 19 or 22. By screening a human chromosome 19 specific genomic cosmid library with a probe from this cDNA sequence, we identified a corresponding cosmid. Portions of this cosmid were sequenced directly. The exon, exon:intron junction and flanking sequences verified that this cosmid contains the genomic locus. Fluorescent in situ hybridization (FISH) was performed to localize this cosmid to chromosome band 19q12. INTRODUCTION Edwards, 1979). The Rieske Fe-S protein is important in redox reactions in these organelles as it is involved in Iron-sulfur (Fe-S) proteins have long been known to electron transport and photosynthesis (Rieske, 1976).
[Show full text]
Orbitofrontal Neuroadaptations and Cross-Species Synaptic Biomarkers in Heavy-Drinking Macaques
3646 • The Journal of Neuroscience, March 29, 2017 • 37(13):3646–3660 Neurobiology of Disease Orbitofrontal Neuroadaptations and Cross-Species Synaptic Biomarkers in Heavy-Drinking Macaques X Sudarat Nimitvilai,1* Joachim D. Uys,2* John J. Woodward,1,3 Patrick K. Randall,3 Lauren E. Ball,2 X Robert W. Williams,4 XByron C. Jones,4 X Lu Lu,4 X Kathleen A. Grant,5 and Patrick J. Mulholland1,3 Departments of 1Neuroscience, 2Cell and Molecular Pharmacology, and 3Psychiatry and Behavioral Sciences, Medical University of South Carolina, Charleston, South Carolina 29425, 4Department of Genetics, Genomics and Informatics, University of Tennessee Health Science Center, Memphis, Tennessee 38120, and 5Department of Behavioral Neuroscience, Oregon Health and Science University, Portland, Oregon 97239 Cognitive impairments, uncontrolled drinking, and neuropathological cortical changes characterize alcohol use disorder. Dysfunction of the orbitofrontal cortex (OFC), a critical cortical subregion that controls learning, decision-making, and prediction of reward outcomes, contributes to executive cognitive function deficits in alcoholic individuals. Electrophysiological and quantitative synaptomics tech- niques were used to test the hypothesis that heavy drinking produces neuroadaptations in the macaque OFC. Integrative bioinformatics and reverse genetic approaches were used to identify and validate synaptic proteins with novel links to heavy drinking in BXD mice. In drinking monkeys, evoked firing of OFC pyramidal neurons was reduced, whereas the amplitude and frequency of postsynaptic currents were enhanced compared with controls. Bath application of alcohol reduced evoked firing in neurons from control monkeys, but not drinking monkeys. Profiling of the OFC synaptome identified alcohol-sensitive proteins that control glutamate release (e.g., SV2A, synaptogyrin-1) and postsynaptic signaling (e.g., GluA1, PRRT2) with no changes in synaptic GABAergic proteins.
[Show full text]
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.
[Show full text]
Mrna-Binding Protein Tristetraprolin Is Essential for Cardiac Response to Iron Deficiency by Regulating Mitochondrial Function
mRNA-binding protein tristetraprolin is essential for 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).
[Show full text]