Citrate Synthase a Mitochondrial Marker Enzyme
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ORIGINAL RESEARCH published: 06 March 2017 doi: 10.3389/fpls.2017.00291 Integrated Transcriptome and Metabolic Analyses Reveals Novel Insights into Free Amino Acid Metabolism in Huangjinya Tea Cultivar Qunfeng Zhang 1, 2, Meiya Liu 1, 2 and Jianyun Ruan 1, 2* 1 Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou, China, 2 Key Laboratory for Plant Biology and Resource Application of Tea, The Ministry of Agriculture, Hangzhou, China The chlorotic tea variety Huangjinya, a natural mutant, contains enhanced levels of free amino acids in its leaves, which improves the drinking quality of its brewed tea. Consequently, this chlorotic mutant has a higher economic value than the non-chlorotic Edited by: varieties. However, the molecular mechanisms behind the increased levels of free amino Basil J. Nikolau, Iowa State University, USA acids in this mutant are mostly unknown, as are the possible effects of this mutation Reviewed by: on the overall metabolome and biosynthetic pathways in tea leaves. To gain further John A. Morgan, insight into the effects of chlorosis on the global metabolome and biosynthetic pathways Purdue University, USA Vinay Kumar, in this mutant, Huangjinya plants were grown under normal and reduced sunlight, Central University of Punjab, India resulting in chlorotic and non-chlorotic leaves, respectively; their leaves were analyzed *Correspondence: using transcriptomics as well as targeted and untargeted metabolomics. Approximately Jianyun Ruan 5,000 genes (8.5% of the total analyzed) and ca. 300 metabolites (14.5% of the total [email protected] detected) were significantly differentially regulated, thus indicating the occurrence of Specialty section: marked effects of light on the biosynthetic pathways in this mutant plant. -
ATP-Citrate Lyase Has an Essential Role in Cytosolic Acetyl-Coa Production in Arabidopsis Beth Leann Fatland Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2002 ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis Beth LeAnn Fatland Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Fatland, Beth LeAnn, "ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis " (2002). Retrospective Theses and Dissertations. 1218. https://lib.dr.iastate.edu/rtd/1218 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis by Beth LeAnn Fatland A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Plant Physiology Program of Study Committee: Eve Syrkin Wurtele (Major Professor) James Colbert Harry Homer Basil Nikolau Martin Spalding Iowa State University Ames, Iowa 2002 UMI Number: 3158393 INFORMATION TO USERS The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. -
Mutation of the Fumarase Gene in Two Siblings with Progressive Encephalopathy and Fumarase Deficiency T
Mutation of the Fumarase Gene in Two Siblings with Progressive Encephalopathy and Fumarase Deficiency T. Bourgeron,* D. Chretien,* J. Poggi-Bach, S. Doonan,' D. Rabier,* P. Letouze,I A. Munnich,* A. R6tig,* P. Landneu,* and P. Rustin* *Unite de Recherches sur les Handicaps Genetiques de l'Enfant, INSERM U393, Departement de Pediatrie et Departement de Biochimie, H6pital des Enfants-Malades, 149, rue de Sevres, 75743 Paris Cedex 15, France; tDepartement de Pediatrie, Service de Neurologie et Laboratoire de Biochimie, Hopital du Kremlin-Bicetre, France; IFaculty ofScience, University ofEast-London, UK; and IService de Pediatrie, Hopital de Dreux, France Abstract chondrial enzyme (7). Human tissue fumarase is almost We report an inborn error of the tricarboxylic acid cycle, fu- equally distributed between the mitochondria, where the en- marase deficiency, in two siblings born to first cousin parents. zyme catalyzes the reversible hydration of fumarate to malate They presented with progressive encephalopathy, dystonia, as a part ofthe tricarboxylic acid cycle, and the cytosol, where it leucopenia, and neutropenia. Elevation oflactate in the cerebro- is involved in the metabolism of the fumarate released by the spinal fluid and high fumarate excretion in the urine led us to urea cycle. The two isoenzymes have quite homologous struc- investigate the activities of the respiratory chain and of the tures. In rat liver, they differ only by the acetylation of the Krebs cycle, and to finally identify fumarase deficiency in these NH2-terminal amino acid of the cytosolic form (8). In all spe- two children. The deficiency was profound and present in all cies investigated so far, the two isoenzymes have been found to tissues investigated, affecting the cytosolic and the mitochon- be encoded by a single gene (9,10). -
Enzyme Phosphatidylserine Synthase (Saccharomyces Cerevisae/Chol Gene/Transformation) V
Proc. Nati. Acad. Sci. USA Vol. 80, pp. 7279-7283, December 1983 Genetics Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase (Saccharomyces cerevisae/CHOl gene/transformation) V. A. LETTS*, L. S. KLIG*, M. BAE-LEEt, G. M. CARMANt, AND S. A. HENRY* *Departments of Genetics and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461; and tDepartment of Food Science, Cook College, New Jersey Agricultural Experimental Station, Rutgers University, New Brunswick, NJ 08903 Communicated by Frank Lilly, August 11, 1983 ABSTRACT The structural gene (CHOI) for phosphatidyl- Mammals, for example, synthesize PtdSer by an exchange re- serine synthase (CDPdiacylglycerol:L-serine O-phosphatidyl- action with PtdEtn (9). However, PtdSer synthase is found in transferase, EC 2.7.8.8) was isolated by genetic complementation E. coli and indeed the structural gene for the E. coli enzyme has in Saccharomyces cerevmae from a bank of yeast genomic DNA been cloned (10). Thus, cloning of the structural gene for the on a chimeric plasmid. The cloned DNA (4.0 kilobases long) was yeast enzyme will permit a detailed comparison of the structure shown to represent a unique sequence in the yeast genome. The and function of prokaryotic and eukaryotic genes and gene DNA sequence on an integrative plasmid was shown to recombine products. The availability of a clone of the CHOI gene will per- into the CHOi locus, confwrming its genetic identity. The chol yeast mit analysis of its regulation at the transcriptional level. Fur- strain transformed with this gene on an autonomously replicating thermore, the cloning of the CHOI gene provides us with the plasmid had significantly increased activity of the regulated mem- the levels of PtdSer synthase in the cell, brane-associated enzyme phosphatidylserine synthase. -
Citric Acid Cycle
CHEM464 / Medh, J.D. The Citric Acid Cycle Citric Acid Cycle: Central Role in Catabolism • Stage II of catabolism involves the conversion of carbohydrates, fats and aminoacids into acetylCoA • In aerobic organisms, citric acid cycle makes up the final stage of catabolism when acetyl CoA is completely oxidized to CO2. • Also called Krebs cycle or tricarboxylic acid (TCA) cycle. • It is a central integrative pathway that harvests chemical energy from biological fuel in the form of electrons in NADH and FADH2 (oxidation is loss of electrons). • NADH and FADH2 transfer electrons via the electron transport chain to final electron acceptor, O2, to form H2O. Entry of Pyruvate into the TCA cycle • Pyruvate is formed in the cytosol as a product of glycolysis • For entry into the TCA cycle, it has to be converted to Acetyl CoA. • Oxidation of pyruvate to acetyl CoA is catalyzed by the pyruvate dehydrogenase complex in the mitochondria • Mitochondria consist of inner and outer membranes and the matrix • Enzymes of the PDH complex and the TCA cycle (except succinate dehydrogenase) are in the matrix • Pyruvate translocase is an antiporter present in the inner mitochondrial membrane that allows entry of a molecule of pyruvate in exchange for a hydroxide ion. 1 CHEM464 / Medh, J.D. The Citric Acid Cycle The Pyruvate Dehydrogenase (PDH) complex • The PDH complex consists of 3 enzymes. They are: pyruvate dehydrogenase (E1), Dihydrolipoyl transacetylase (E2) and dihydrolipoyl dehydrogenase (E3). • It has 5 cofactors: CoASH, NAD+, lipoamide, TPP and FAD. CoASH and NAD+ participate stoichiometrically in the reaction, the other 3 cofactors have catalytic functions. -
Differential Regulation of Cysteine Oxidative Post-Translational
www.nature.com/scientificreports OPEN Diferential regulation of cysteine oxidative post-translational modifcations in high and low Received: 16 April 2018 Accepted: 9 October 2018 aerobic capacity Published: xx xx xxxx Rodrigo W. A. Souza1, Christiano R. R. Alves 1,2, Alessandra Medeiros3, Natale Rolim4, Gustavo J. J. Silva4, José B. N. Moreira4, Marcia N. Alves4, Martin Wohlwend4, Mohammed Gebriel5, Lars Hagen5, Animesh Sharma 5, Lauren G. Koch6, Steven L. Britton7,8, Geir Slupphaug5, Ulrik Wisløf4,9 & Patricia C. Brum 1 Given the association between high aerobic capacity and the prevention of metabolic diseases, elucidating the mechanisms by which high aerobic capacity regulates whole-body metabolic homeostasis is a major research challenge. Oxidative post-translational modifcations (Ox-PTMs) of proteins can regulate cellular homeostasis in skeletal and cardiac muscles, but the relationship between Ox-PTMs and intrinsic components of oxidative energy metabolism is still unclear. Here, we evaluated the Ox-PTM profle in cardiac and skeletal muscles of rats bred for low (LCR) and high (HCR) intrinsic aerobic capacity. Redox proteomics screening revealed diferent cysteine (Cys) Ox-PTM profle between HCR and LCR rats. HCR showed a higher number of oxidized Cys residues in skeletal muscle compared to LCR, while the opposite was observed in the heart. Most proteins with diferentially oxidized Cys residues in the skeletal muscle are important regulators of oxidative metabolism. The most oxidized protein in the skeletal muscle of HCR rats was malate dehydrogenase (MDH1). HCR showed higher MDH1 activity compared to LCR in skeletal, but not cardiac muscle. These novel fndings indicate a clear association between Cys Ox-PTMs and aerobic capacity, leading to novel insights into the role of Ox- PTMs as an essential signal to maintain metabolic homeostasis. -
Assembly of the Membrane Domain of ATP Synthase in Human Mitochondria
Assembly of the membrane domain of ATP synthase in human mitochondria Jiuya Hea,1, Holly C. Forda,1, Joe Carrolla, Corsten Douglasa, Evvia Gonzalesa, Shujing Dinga, Ian M. Fearnleya, and John E. Walkera,2 aMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom Contributed by John E. Walker, January 16, 2018 (sent for review December 20, 2017; reviewed by Ulrich Brandt and Nikolaus Pfanner) The ATP synthase in human mitochondria is a membrane-bound mitochondria in human ρ0 cells lack organellar DNA and contain assembly of 29 proteins of 18 kinds. All but two membrane another incomplete ATP synthase, necessarily with no ATP6 or components are encoded in nuclear genes, synthesized on cyto- ATP8 (7, 9). These incomplete vestigial ATP synthases provide plasmic ribosomes, and imported into the matrix of the organelle, insight into the pathway of assembly of the complete enzyme. where they are assembled into the complex with ATP6 and ATP8, Here we investigated the effects of the selective removal of su- the products of overlapping genes in mitochondrial DNA. Disrup- pernumerary membrane subunits e, f, g, DAPIT, and 6.8PL on tion of individual human genes for the nuclear-encoded subunits assembly of human ATP synthase. in the membrane portion of the enzyme leads to the formation of intermediate vestigial ATPase complexes that provide a descrip- Results tion of the pathway of assembly of the membrane domain. The Human Cells Lacking Supernumerary Subunits. The human genes key intermediate complex consists of the F1-c8 complex inhibited ATP5I, ATP5J2, ATP5L, USMG5, and C14orf2 (SI Appendix, Fig. -
Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase -
Relationships Between Expression of BCS1L, Mitochondrial Bioenergetics, and Fatigue Among Patients with Prostate Cancer
Cancer Management and Research Dovepress open access to scientific and medical research Open Access Full Text Article ORIGINAL RESEARCH Relationships between expression of BCS1L, mitochondrial bioenergetics, and fatigue among patients with prostate cancer This article was published in the following Dove Press journal: Cancer Management and Research Chao-Pin Hsiao1,2 Introduction: Cancer-related fatigue (CRF) is the most debilitating symptom with the Mei-Kuang Chen3 greatest adverse side effect on quality of life. The etiology of this symptom is still not Martina L Veigl4 understood. The purpose of this study was to examine the relationship between mitochon- Rodney Ellis5 drial gene expression, mitochondrial oxidative phosphorylation, electron transport chain Matthew Cooney6 complex activity, and fatigue in prostate cancer patients undergoing radiotherapy (XRT), Barbara Daly1 compared to patients on active surveillance (AS). Methods: The study used a matched case–control and repeated-measures research design. Charles Hoppel7 Fatigue was measured using the revised Piper Fatigue Scale from 52 patients with prostate 1The Frances Payne Bolton School of cancer. Mitochondrial oxidative phosphorylation, electron-transport chain enzymatic activity, Nursing, Case Western Reserve ’ University, Cleveland, OH, USA; 2School and BCS1L gene expression were determined using patients peripheral mononuclear cells. of Nursing, Taipei Medical University, Data were collected at three time points and analyzed using repeated measures ANOVA. 3 Taipei , Taiwan; Department of Results: The fatigue score was significantly different over time between patients undergoing XRT Psychology, University of Arizona, fi Tucson, AZ, USA; 4Gene Expression & and AS (P<0.05). Patients undergoing XRT experienced signi cantly increased fatigue at day 21 Genotyping Facility, Case Comprehensive and day 42 of XRT (P<0.01). -
Apoptosis Induced by Microinjection of Cytochrome C Is Caspase-Dependent and Is Inhibited by Bcl-2
Cell Death and Differentiation (1998) 5, 660 ± 668 1998 Stockton Press All rights reserved 13509047/98 $12.00 http://www.stockton-press.co.uk/cdd Apoptosis induced by microinjection of cytochrome c is caspase-dependent and is inhibited by Bcl-2 Odd T. Brustugun1, Kari E. Fladmark1, Stein O. Dùskeland1,3, proteins, chromatin and RNA degradation, cell shrinkage and Sten Orrenius2 and Boris Zhivotovsky2 blebbing of cell membranes accompanied by the appearance of phosphatidyl serine on the outer surface of the plasma 1 Department of Anatomy and Cell Biology, University of Bergen, AÊ rstadveien 19, membrane. N-5009 Bergen, Norway The biochemical machinery involved in the killing and 2 Institute of Environmental Medicine, Division of Toxicology, Karolinska degradation of the cell is constitutively expressed. During Institutet, Box 210, S-171 77 Stockholm, Sweden the last few years the `main players' in the induction and 3 corresponding author: Department of Anatomy and Cell Biology, University of execution cascade of reactions in apoptotic cells were Bergen, AÊ rstadveien 19, N-5009 Bergen, Norway. tel: +47 55 58 63 76; fax: +47 55 58 63 60; e-mail: [email protected] identified as a family of aspartic acid-specific cysteine proteases, the caspases (Alnemri et al, 1996). Over- Received 26.11.97; revised 2.3.98; accepted 23.3.98 expression of any of these proteases leads to apoptotic Edited by G. Melino cell death. Moreover, mice deficient in caspase-3 have a striking defect in the extensive apoptosis that occurs during brain development. Peptide inhibitors of caspases can Abstract prevent apoptosis both in isolated cells and in in vivo Microinjection of cytochrome c induced apoptosis in all the models of development. -
Aconitase: to Be Or Not to Be Inside Plant Glyoxysomes, That Is the Question
biology Review Aconitase: To Be or not to Be Inside Plant Glyoxysomes, That Is the Question Luigi De Bellis 1,* , Andrea Luvisi 1 and Amedeo Alpi 2 1 Department of Biological and Environmental Sciences and Technologies, University of Salento, Via Prov. le Monteroni, I-73100 Lecce, Italy; [email protected] 2 Approaching Research Educational Activities (A.R.E.A.) Foundation, I-56126 Pisa, Italy; [email protected] * Correspondence: [email protected] Received: 10 June 2020; Accepted: 10 July 2020; Published: 12 July 2020 Abstract: After the discovery in 1967 of plant glyoxysomes, aconitase, one the five enzymes involved in the glyoxylate cycle, was thought to be present in the organelles, and although this was found not to be the case around 25 years ago, it is still suggested in some textbooks and recent scientific articles. Genetic research (including the study of mutants and transcriptomic analysis) is becoming increasingly important in plant biology, so metabolic pathways must be presented correctly to avoid misinterpretation and the dissemination of bad science. The focus of our study is therefore aconitase, from its first localization inside the glyoxysomes to its relocation. We also examine data concerning the role of the enzyme malate dehydrogenase in the glyoxylate cycle and data of the expression of aconitase genes in Arabidopsis and other selected higher plants. We then propose a new model concerning the interaction between glyoxysomes, mitochondria and cytosol in cotyledons or endosperm during the germination of oil-rich seeds. Keywords: aconitase; malate dehydrogenase; glyoxylate cycle; glyoxysomes; peroxisomes; β-oxidation; gluconeogenesis 1. Introduction Glyoxysomes are specialized types of plant peroxisomes containing glyoxylate cycle enzymes, which participate in the conversion of lipids to sugar during the early stages of germination in oilseeds. -
Bax Transmembrane Domain Interacts with Prosurvival Bcl-2 Proteins in Biological Membranes
Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes Vicente Andreu-Fernándeza,b,c, Mónica Sanchoa, Ainhoa Genovésa, Estefanía Lucendoa, Franziska Todtb, Joachim Lauterwasserb,d, Kathrin Funkb,d, Günther Jahreise, Enrique Pérez-Payáa,f,1, Ismael Mingarroc,2, Frank Edlichb,g,2, and Mar Orzáeza,2 aLaboratory of Peptide and Protein Chemistry, Centro de Investigación Príncipe Felipe, E-46012 Valencia, Spain; bInstitute for Biochemistry and Molecular Biology, University of Freiburg, 79104 Freiburg, Germany; cDepartament de Bioquímica i Biologia Molecular, Estructura de Recerca Interdisciplinar en Biotecnología i Biomedicina, Universitat de València, 46100 Burjassot, Spain; dFaculty of Biology, University of Freiburg, 79104 Freiburg, Germany; eDepartment of Biochemistry/Biotechnology, Martin Luther University Halle-Wittenberg, 06120 Halle, Germany; fInstituto de Biomedicina de Valencia, Instituto de Biomedicina de Valencia–Consejo Superior de Investigaciones Científicas, 46010 Valencia, Spain; and gBIOSS, Centre for Biological Signaling Studies, University of Freiburg, 79104 Freiburg, Germany Edited by William F. DeGrado, School of Pharmacy, University of California, San Francisco, CA, and approved November 29, 2016 (received for review July 28, 2016) The Bcl-2 (B-cell lymphoma 2) protein Bax (Bcl-2 associated X, across bilayers via changes in the oligomeric state or protein con- apoptosis regulator) can commit cells to apoptosis via outer mito- formation (22–24). The Bax TMD targets fusion proteins to the chondrial membrane permeabilization. Bax activity is controlled in OMM; its deletion results in cytosolic Bax localization and impaired healthy cells by prosurvival Bcl-2 proteins. C-terminal Bax trans- Bax activity (25). Analysis of the active Bax membrane topology membrane domain interactions were implicated recently in Bax pore suggests that the TMD could play a central role in Bax oligomeri- formation.