<I>Cucumis Melo</I>

Total Page:16

File Type:pdf, Size:1020Kb

<I>Cucumis Melo</I> University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Agronomy & Horticulture -- Faculty Publications Agronomy and Horticulture Department 2014 Transcriptomic and physiological characterization of the fefe mutant of melon (Cucumis melo) reveals new aspects of iron-copper crosstalk Brian M. Waters University of Nebraska-Lincoln, [email protected] Samuel A. McInturf University of Nebraska-Lincoln Keenan Amundsen University of Nebraska-Lincoln, [email protected] Follow this and additional works at: https://digitalcommons.unl.edu/agronomyfacpub Part of the Agricultural Science Commons, Agriculture Commons, Agronomy and Crop Sciences Commons, Botany Commons, Horticulture Commons, Other Plant Sciences Commons, and the Plant Biology Commons Waters, Brian M.; McInturf, Samuel A.; and Amundsen, Keenan, "Transcriptomic and physiological characterization of the fefe mutant of melon (Cucumis melo) reveals new aspects of iron-copper crosstalk" (2014). Agronomy & Horticulture -- Faculty Publications. 829. https://digitalcommons.unl.edu/agronomyfacpub/829 This Article is brought to you for free and open access by the Agronomy and Horticulture Department at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Agronomy & Horticulture -- Faculty Publications by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Published in New Phytologist 203 (2014), pp. 1128–1145; doi: 10.1111/nph.12911 Copyright © 2014 Brian M. Waters, Samuel A. McInturf, and Keenan Amundsen. Used by permission. New Phytologist © 2014 New Phytologist Trust; published by John Wiley & Sons. Submitted February 3, 2014; accepted May 9, 2014 digitalcommons.unl.edudigitalcommons.unl.edu Supporting information for this article follows the references. Transcriptomic and physiological characterization of the fefe mutant of melon (Cucumis melo) reveals new aspects of iron-copper crosstalk Brian M. Waters, Samuel A. McInturf and Keenan Amundsen Department of Agronomy and Horticulture, University of Nebraska, Lincoln NE 68583-0915, USA Corresponding author – Brian M. Waters, email [email protected] Abstract Iron (Fe) and copper (Cu) homeostasis are tightly linked across biology. In previous work, Fe deficiency interacted with Cu-regu- lated genes and stimulated Cu accumulation. The C940-fe (fefe) Fe-uptake mutant of melon (Cucumis melo) was characterized, and the fefe mutant was used to test whether Cu deficiency could stimulate Fe uptake. Wild-type and fefe mutant transcriptomes were determined by RNA-seq under Fe and Cu deficiency. FeFe-regulated genes included core Fe uptake, metal homeostasis, and tran- scription factor genes. Numerous genes were regulated by both Fe and Cu. The fefe mutant was rescued by high Fe or by Cu defi- ciency, which stimulated ferric-chelate reductase activity, FRO2 expression, and Fe accumulation. Accumulation of Fe in Cu-de- ficient plants was independent of the normal Fe-uptake system. One of the four FRO genes in the melon and cucumber (Cucumis sativus) genomes was Fe-regulated, and one was Cu-regulated. Simultaneous Fe and Cu deficiency synergistically up-regulated Fe-uptake gene expression. Overlap in Fe and Cu deficiency transcriptomes highlights the importance of Fe-Cu crosstalk in metal homeostasis. The fefe gene is not orthologous to FIT, and thus identification of this gene will provide clues to help understand reg- ulation of Fe uptake in plants. Keywords: copper (Cu), fefe mutant, ferricchelate reductase, iron (Fe), iron-copper crosstalk, melon (Cucumis melo), metal homeostasis Introduction and bHLH039 (Yuan et al., 2008; Wang et al., 2013), and these proteins also have regulatory roles independent of FIT (Siv- Iron (Fe) and copper (Cu) are trace metals that are required by itz et al., 2012; Wang et al., 2013). Several metal homeostasis plants for their roles in redox metabolism, such as mitochon- genes respond to both Fe and Cu, such as the metal transport- drial respiration, photosynthesis, and nitrogen fixation (Puig ers COPT2 and ZIP2, and the ferric-chelate reductase FRO3 et al., 2007; Burkhead et al., 2009; Hansch & Mendel, 2009; Pi- (Sancenon et al., 2003; Wintz et al., 2003; Colangelo & Gueri- lon et al., 2011). Excess Fe or Cu leads to oxidative stress and not, 2004; Mukherjee et al., 2006; Buckhout et al., 2009; Garcia damage from reactive oxygen species (Halliwell & Gutter- et al., 2010; del Pozo et al., 2010; Yang et al., 2010; Stein & Wa- idge, 1992). However, Fe and Cu are both involved in protec- ters, 2012; Waters et al., 2012). Similarly, Cu deficiency results tion from reactive oxygen species (Hansch & Mendel, 2009) in up-regulated ferric-chelate reductase activity in roots (Nor- as components of peroxidases, catalase, and superoxide dis- vell et al., 1993; Welch et al., 1993; Cohen et al., 1997; Romera mutases (SODs). Iron-containing SODs (FeSODs) and Cu- et al., 2003; Chen et al., 2004). Arabidopsis FRO4 and FRO5 are containing SODs (CuSODs) are functionally interchangeable, up-regulated by Cu deficiency but not by Fe deficiency (Bernal but are products of different genes (Kliebenstein et al., 1998; et al., 2012), and provide low-level but significant ferricchelate Alscher et al., 2002; Myouga et al., 2008; Pilon et al., 2011). reductase activity. Iron deficiency responses include increased expression of Changes in availability of one mineral nutrient often results certain genes to increase Fe uptake and to make cellular ad- in changes in homeostasis of other minerals. For example, Fe justments to maintain homeostasis. The basic helix-loop-helix deficiency caused changes in the expression of genes related to (bHLH) transcription factor FIT is required for normal regula- potassium and phosphate (Wang et al., 2002) and sulfate (Pao- tion of Fe-uptake genes in Arabidopsis (Colangelo & Guerinot, lacci et al., 2013) homeostasis. Fe homeostasis interacts with 2004; Jakoby et al., 2004), including the ferric-chelate reductase Zn tolerance (Pineau et al., 2012), and Cu deficiency interacts FRO2, the primary Fe transporter IRT1, and another Fe trans- with phosphate signaling (Perea-García et al., 2013) and cad- porter, NRAMP1. The FIT protein interacts with other Fe-regu- mium tolerance (Gayomba et al., 2013). Copper concentration lated bHLH proteins, such as bHLH100, bHLH101, bHLH038, was higher in Fe-deficient leaves (Welch et al., 1993; Chaignon 1128 T RANSCRIP T OMIC AND PHYSIOLOGICAL CHARAC T ERIZA T ION OF T HE FEFE MU T AN T OF MELON 1129 et al., 2002; Waters & Troupe, 2012; Waters et al., 2012). Sev- EDDHA (Sprint 138, Becker-Underwood, Ames, IA, USA), eral Cu-responsive genes and microRNAs had altered abun- 25 µM CaCl2, 25µM H3BO3, 2µM MnCl2, 2µM ZnSO4, 0.5 µM dance under Fe deficiency in Arabidopsis thaliana (Stein & Wa- CuSO4, 0.5 µM Na2MoO4 and 1 mM MES buffer (pH 5.5) or, ters, 2012; Waters et al., 2012). This suggested that a specific if indicated, HEPES buffer (pH 7.1). Fe was omitted or sup- role for accumulation of Cu under Fe deficiency is the replace- plied as indicated for Fe-supply treatments, and Cu was omit- ment of FeSOD, which decreases under Fe deficiency (Kurepa ted or supplied as indicated for Cu-supply treatments. For N et al., 1997; Waters et al., 2012), with CuSOD, whose tran- source experiments, the same micronutrients were used, with scripts increase in Fe-deficient leaves (Waters et al., 2012). Sup- a macronutrient solution as follows: 0.7mM K2SO4, 0.1mM porting this hypothesis, counteraction of oxidative stress was KH2PO4, 0.1mM KCl, 0.5mM MgSO4, and 1 mM CaCl2. Nitro- impaired when formation of functional CuSOD protein was gen was added at a final concentration of 2.5mM as (NH4)2SO4 blocked under Fe deficiency (Waters et al., 2012). Increasing or KNO3. evidence points to the importance of Fe-Cu crosstalk in metal Melon and cucumber seeds were sprouted on germina- homeostasis (Bernal et al., 2012; Waters et al., 2012; Perea-Gar- tion paper in a 30°C incubator until transplanting to hydro- cía et al., 2013). ponics after 4 d. Seedlings were placed in sponge holders in Mutant lines with altered metal homeostasis are valu- lids of black plastic containers, four plants per 750 ml solu- able tools to study molecular and physiological responses to tion. Plants were grown in a growth chamber with a mix of metal stress. The fefe mutation originated spontaneously in the incandescent and fluorescent light at 300 µmol m–2s–1. For melon (Cucumis melo) variety Edisto, and was crossed into the cucumber, plants were pretreated in standard solution for variety Mainstream to generate the C940-fe germplasm (Nu- 5 d before nutrient treatments for 3 d. For the –Cu fefe mu- gent & Bhella, 1988; Nugent, 1994). The fefe mutant lacks ferric- tant rescue and WT controls, seedlings were grown without chelate reductase activity and rhizosphere acidification (Jolley Cu from initial planting for 9 d. Plants for the +/– Cu RNA- et al., 1991), two of the important mechanisms of the reductive seq experiment (Edisto and fefe) were collected at 9 d. For the strategy of Fe uptake in dicots and nongrass monocots. The fefe +/– Fe RNA-seq experiment, WT (Edisto and snake melon) mutant has chlorotic leaves typical of Fe deficiency, which can and fefe mutants were pretreated for 9 d on –Cu solution, and be corrected by application of external Fe. These signs point to only fefe mutants that had green leaves were used for treat- fefe as a regulator of Fe uptake, but the mutant was not fully ments of 3 d duration. The purpose of the –Cu pretreatment physiologically characterized to determine if the mutation is was to use only healthy fefe plants so that the transcriptome specific to root function. Additionally, gene expression levels would reflect the Fe-regulated genes in fefe rather than sec- in fefe had not been characterized. ondary effects of severe Fe deficiency. To avoid potential Our overall objective in this study was to use the fefe mu- variation resulting from the circadian clock, sampling for fer- tant to increase understanding of Fe-uptake regulation and to ric-chelate reductase activity or RNA was always performed explore Fe-Cu crosstalk through characterization of transcrip- between 14:00 and 16:00 h.
Recommended publications
  • Ferric Reductase Activity of the Arsh Protein from Acidithiobacillus Ferrooxidans
    J. Microbiol. Biotechnol. (2011), 21(5), 464–469 doi: 10.4014/jmb.1101.01020 First published online 13 April 2011 Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans Mo, Hongyu1,2, Qian Chen1,2, Juan Du1, Lin Tang1, Fang Qin1, Bo Miao2, Xueling Wu2, and Jia Zeng1,2* 1College of Biology, Hunan University, Changsha, Hunan 410082, P. R. China 2Department of Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China Received: January 14, 2011 / Revised: March 10, 2011 / Accepted: March 11, 2011 The arsH gene is one of the arsenic resistance system in iron (free or chelated) into ferrous iron before its incorporation bacteria and eukaryotes. The ArsH protein was annotated into heme and nonheme iron-containing proteins. Ferric as a NADPH-dependent flavin mononucleotide (FMN) reductase catalyzes the reduction of complexed Fe3+ to reductase with unknown biological function. Here we complexed Fe2+ using NAD(P)H as the electron donor. The report for the first time that the ArsH protein showed resulting Fe2+ is subsequently released and incorporated high ferric reductase activity. Glu104 was an essential into iron-containing proteins [17]. residue for maintaining the stability of the FMN cofactor. Here we report for the first time that the ArsH protein The ArsH protein may perform an important role for showed high ferric reduction activity. The ArsH from A. cytosolic ferric iron assimilation in vivo. ferrooxidans may perform an important role as a NADPH- Keywords: Acidithiobacillus ferrooxidans, ArsH, flavoprotein, dependent ferric reductase for cytosolic ferric iron assimilation ferric reductase in vivo. MATERIALS AND METHODS Arsenic resistance genes are widespread in nature.
    [Show full text]
  • Molecular Regulation of Plant Monoterpene Biosynthesis in Relation to Fragrance
    Molecular Regulation of Plant Monoterpene Biosynthesis In Relation To Fragrance Mazen K. El Tamer Promotor: Prof. Dr. A.G.J Voragen, hoogleraar in de Levensmiddelenchemie, Wageningen Universiteit Co-promotoren: Dr. ir. H.J Bouwmeester, senior onderzoeker, Business Unit Celcybernetica, Plant Research International Dr. ir. J.P Roozen, departement Agrotechnologie en Voedingswetenschappen, Wageningen Universiteit Promotiecommissie: Dr. M.C.R Franssen, Wageningen Universiteit Prof. Dr. J.H.A Kroeze, Wageningen Universiteit Prof. Dr. A.J van Tunen, Swammerdam Institute for Life Sciences, Universiteit van Amsterdam. Prof. Dr. R.G.F Visser, Wageningen Universiteit Mazen K. El Tamer Molecular Regulation Of Plant Monoterpene Biosynthesis In Relation To Fragrance Proefschrift ter verkrijging van de graad van doctor op gezag van de rector magnificus van Wageningen Universiteit, Prof. dr. ir. L. Speelman, in het openbaar te verdedigen op woensdag 27 november 2002 des namiddags te vier uur in de Aula Mazen K. El Tamer Molecular Regulation Of Plant Monoterpene Biosynthesis In Relation To Fragrance Proefschrift Wageningen Universiteit ISBN 90-5808-752-2 Cover and Invitation Design: Zeina K. El Tamer This thesis is dedicated to my Family & Friends Contents Abbreviations Chapter 1 General introduction and scope of the thesis 1 Chapter 2 Monoterpene biosynthesis in lemon (Citrus limon) cDNA isolation 21 and functional analysis of four monoterpene synthases Chapter 3 Domain swapping of Citrus limon monoterpene synthases: Impact 57 on enzymatic activity and
    [Show full text]
  • Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: from Structure, Functions to Applications
    International Journal of Molecular Sciences Review Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: From Structure, Functions to Applications Kai Hong , Limin Wang, Agbaka Johnpaul , Chenyan Lv * and Changwei Ma * College of Food Science and Nutritional Engineering, China Agricultural University, 17 Qinghua Donglu Road, Haidian District, Beijing 100083, China; [email protected] (K.H.); [email protected] (L.W.); [email protected] (A.J.) * Correspondence: [email protected] (C.L.); [email protected] (C.M.); Tel./Fax: +86-10-62737643 (C.M.) Abstract: Humulus lupulus L. is an essential source of aroma compounds, hop bitter acids, and xanthohumol derivatives mainly exploited as flavourings in beer brewing and with demonstrated potential for the treatment of certain diseases. To acquire a comprehensive understanding of the biosynthesis of these compounds, the primary enzymes involved in the three major pathways of hops’ phytochemical composition are herein critically summarized. Hops’ phytochemical components impart bitterness, aroma, and antioxidant activity to beers. The biosynthesis pathways have been extensively studied and enzymes play essential roles in the processes. Here, we introduced the enzymes involved in the biosynthesis of hop bitter acids, monoterpenes and xanthohumol deriva- tives, including the branched-chain aminotransferase (BCAT), branched-chain keto-acid dehydroge- nase (BCKDH), carboxyl CoA ligase (CCL), valerophenone synthase (VPS), prenyltransferase (PT), 1-deoxyxylulose-5-phosphate synthase (DXS), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), Geranyl diphosphate synthase (GPPS), monoterpene synthase enzymes (MTS), cinnamate Citation: Hong, K.; Wang, L.; 4-hydroxylase (C4H), chalcone synthase (CHS_H1), chalcone isomerase (CHI)-like proteins (CHIL), Johnpaul, A.; Lv, C.; Ma, C.
    [Show full text]
  • Bioprospecting for Hydroxynitrile Lyases by Blue Native PAGE Coupled HCN Detection
    Send Orders for Reprints to [email protected] Current Biotechnology, 2015, 4, 111-117 111 Bioprospecting for Hydroxynitrile Lyases by Blue Native PAGE Coupled HCN Detection Elisa Lanfranchi1, Eva-Maria Köhler1, Barbara Darnhofer1,2,3, Kerstin Steiner1, Ruth Birner-Gruenberger1,2,3, Anton Glieder1,4 and Margit Winkler*,1 1ACIB GmbH, Graz, Austria; 2Institute for Pathology, Medical University of Graz, Graz, Austria; 3Omics Center Graz, BioTechMed, Graz, Austria; 4Institute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Graz, Austria Abstract: Hydroxynitrile lyase enzymes (HNLs) catalyze the stereoselective addition of HCN to carbonyl compounds to give valuable chiral hydroxynitriles. The discovery of new sources of HNL activity has been reported several times as the result of extensive screening of diverse plants for cyanogenic activity. Herein we report a two step-method that allows estimation of not only the native size of the active HNL enzyme but also its substrate specificity. Specifically, crude protein extracts from plant tissue are first subjected to blue native-PAGE. The resulting gel is then directly used for an activity assay in which the formation of hydrocyanic acid (HCN) is detected upon the cyanogenesis reaction of any cyanohydrin catalyzed by the enzyme of interest. The same gel may be used with different substrates, thus exploring the enzyme’s substrate scope already on the screening level. In combination with mass spectrometry, sequence information can be retrieved, which is demonstrated
    [Show full text]
  • ADHERENCE and ALKALINIZATION by Elizabeth Hwang
    TWO EARLY PROCESSES DURING INFECTION BY THE FUNGAL PATHOGEN CANDIDA GLABRATA: ADHERENCE AND ALKALINIZATION By Elizabeth Hwang-Wong A dissertation submitted to Johns Hopkins University in conformity with the requirements for the degree of Doctor of Philosophy Baltimore, Maryland November, 2016 Abstract Candida glabrata is a yeast pathogen of increasing diagnostic incidence. Its intrinsic resistance to antifungal agents used in standard clinical settings compels a need to further characterize and understand the pathogenesis of this species. The ability of C. glabrata to adhere to both abiotic surfaces and host cells is an essential early step in establishment of infection. It is also postulated that the capability of this pathogen to externally alkalinize an acidic environment, such as that found within an immune effector’s phagolysosome, could provide an evasive mechanism to resist initial onslaught of an innate immune response. Members of a major class of adhesins encoded by the C. glabrata genome were previously described as Epithelial Adhesins (Epas). Earlier studies have demonstrated the existence of more than 20 members of this class, many of which are encoded in subtelomeric regions of the pathogen’s genome. A major sequencing project has now defined a total complement of 25 members, a newly described one of which is shown to function as a major adhesin across multiple host cell types. In fact, functional adherence of all putative adhesins encoded in the subtelomeres of C. glabrata has been tested, and with minor exception, all are EPAs. The ligand specificities of these functional adhesins were further tested utilizing glycan arrays, and revealed clues identifying a specific EPA responsible for mediating adherence to macrophages.
    [Show full text]
  • The HOTHEAD Protein: Assessing Enzymatic Activity Using Computational and Recombinant Protein Expression Approaches
    The HOTHEAD Protein: Assessing Enzymatic Activity using Computational and Recombinant Protein Expression Approaches By Eric Le Dreff-Kerwin A thesis Presented to the University of Waterloo In fulfillment of the Thesis requirement for the degree of Master of Science In Biology Waterloo, Ontario, Canada, 2019 © Eric Le Dreff-Kerwin 2019 Author’s Declaration I hereby declare that I am the sole author of this thesis. This is a true copy of the thesis, including any required final revisions, as accepted by my examiners. I understand that my thesis may be made electronically available to the public. ii Abstract In Arabidopsis thaliana, a number of genes regulating cuticle synthesis have been identified by virtue of organ fusion phenotype. One such gene, HOTHEAD (HTH) was among those originally identified by this phenotype but its exact role in cuticle formation has proven challenging to determine. Previous bioinformatic work has identified that the HTH protein is a member of the GMC oxidoreductase family, and shares peptide sequence identity with a mandelonitrile lyase and an alcohol dehydrogenase that are within the same protein family. This thesis work investigated the potential enzymatic function of HTH by comparing a structural model to two structural analogs. The structure model of HTH, as determined in this study, shows that HTH shares certain conserved features of GMC proteins. The aim of this research also included isolating a recombinantly expressed HTH protein from Escherichia coli and initial work in Pichia pastoris. Protein isolation attempts in Escherichia coli failed to yield active HTH protein, potentially due to the lack of post-translational modifications.
    [Show full text]
  • Corynebacterium Glutamicum Mycoredoxin 3 Protects Against Multiple Oxidative Stresses
    Advance Publication J. Gen. Appl. Microbiol. doi 10.2323/jgam.2019.10.003 ©2020 Applied Microbiology, Molecular and Cellular Biosciences Research Foundation Full Paper 1 Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses 2 and displays thioredoxin-like activity 3 (Received September 24, 2019; Accepted October 28, 2019; J-STAGE Advance publication date: October 30, 2020) 4 Tao Su#, Chengchuan Che#, Ping Sun, Xiaona Li, Zhijin Gong, Jinfeng Liu, Ge Yang * 5 6 College of Life Sciences, Qufu Normal University, Qufu, Shandong 273165, China; 7 8 Running title: Feature of C. glutamicum mycoredoxin 3 9 10 11 # These authors contributed equally to this work. 12 13 * Corresponding authors: 14 Ge Yang 15 16 E-mail [email protected] 17 Tel: 86-13953760056 18 19 20 21 22 23 24 25 26 27 Abstract 28 Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative 29 conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a 30 high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. 31 Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection 32 against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in 33 ribonucleotide reductase (RNR), insulin and 5, 5’-dithiobis-(2-nitro-benzoicacid) (DTNB), but 34 also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was 35 exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol 36 mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 37 were necessary to maintain its activity.
    [Show full text]
  • Generate Metabolic Map Poster
    Authors: Peter D. Karp Suzanne Paley Julio Collado-Vides John L Ingraham Ingrid Keseler Markus Krummenacker Cesar Bonavides-Martinez Robert Gunsalus An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Carol Fulcher Ian Paulsen Socorro Gama-Castro Robert LaRossa Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. EcoCyc: Escherichia coli K-12 substr. MG1655 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari Amanda Mackie Alberto Santos-Zavaleta succinate phosphate succinate N-acetyl-DL-methionine + L-ornithine glutathione + L-methionine S-oxide D-fructofuranose γ Ag+ molybdate ferroheme b L,L-homocystine asp lys cys L-alanyl- -D- D-mannopyranose 6-phosphate 2+ 2+ H D-methionine 2-deoxy-D-glucose succinate formate formate succinate D-tartrate putrescine agmatine cadaverine L-tartrate D-fructofuranose 6-phosphate + nitrate nitrate Cu thiosulfate deoxycholate L,L-homocystine D-cystine D-cycloserine methyl β-D-glucoside putrescine asp spermidine (S)-2-hydroxybutanoate (S)-2-hydroxybutanoate arg L-homoserine lactone magnesium hydrogenphosphate magnesium hydrogenphosphate antimonous acid glutamyl-meso- Co2+ Cd2+ lactulose poly-β-1,6- met cob(I)inamide 2,3-dioxo-
    [Show full text]
  • Generate Metabolic Map Poster
    Authors: Pallavi Subhraveti Anamika Kothari Quang Ong Ron Caspi An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Peter D Karp Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Csac1394711Cyc: Candidatus Saccharibacteria bacterium RAAC3_TM7_1 Cellular Overview Connections between pathways are omitted for legibility. Tim Holland TM7C00001G0420 TM7C00001G0109 TM7C00001G0953 TM7C00001G0666 TM7C00001G0203 TM7C00001G0886 TM7C00001G0113 TM7C00001G0247 TM7C00001G0735 TM7C00001G0001 TM7C00001G0509 TM7C00001G0264 TM7C00001G0176 TM7C00001G0342 TM7C00001G0055 TM7C00001G0120 TM7C00001G0642 TM7C00001G0837 TM7C00001G0101 TM7C00001G0559 TM7C00001G0810 TM7C00001G0656 TM7C00001G0180 TM7C00001G0742 TM7C00001G0128 TM7C00001G0831 TM7C00001G0517 TM7C00001G0238 TM7C00001G0079 TM7C00001G0111 TM7C00001G0961 TM7C00001G0743 TM7C00001G0893 TM7C00001G0630 TM7C00001G0360 TM7C00001G0616 TM7C00001G0162 TM7C00001G0006 TM7C00001G0365 TM7C00001G0596 TM7C00001G0141 TM7C00001G0689 TM7C00001G0273 TM7C00001G0126 TM7C00001G0717 TM7C00001G0110 TM7C00001G0278 TM7C00001G0734 TM7C00001G0444 TM7C00001G0019 TM7C00001G0381 TM7C00001G0874 TM7C00001G0318 TM7C00001G0451 TM7C00001G0306 TM7C00001G0928 TM7C00001G0622 TM7C00001G0150 TM7C00001G0439 TM7C00001G0233 TM7C00001G0462 TM7C00001G0421 TM7C00001G0220 TM7C00001G0276 TM7C00001G0054 TM7C00001G0419 TM7C00001G0252 TM7C00001G0592 TM7C00001G0628 TM7C00001G0200 TM7C00001G0709 TM7C00001G0025 TM7C00001G0846 TM7C00001G0163 TM7C00001G0142 TM7C00001G0895 TM7C00001G0930 Detoxification Carbohydrate Biosynthesis DNA combined with a 2'- di-trans,octa-cis a 2'- Amino Acid Degradation an L-methionyl- TM7C00001G0190 superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E.
    [Show full text]
  • The Human Flavoproteome
    CORE Metadata, citation and similar papers at core.ac.uk Provided by Elsevier - Publisher Connector Archives of Biochemistry and Biophysics 535 (2013) 150–162 Contents lists available at SciVerse ScienceDirect Archives of Biochemistry and Biophysics journal homepage: www.elsevier.com/locate/yabbi Review The human flavoproteome ⇑ Wolf-Dieter Lienhart, Venugopal Gudipati, Peter Macheroux Graz University of Technology, Institute of Biochemistry, Petersgasse 12, A-8010 Graz, Austria article info abstract Article history: Vitamin B2 (riboflavin) is an essential dietary compound used for the enzymatic biosynthesis of FMN and Received 17 December 2012 FAD. The human genome contains 90 genes encoding for flavin-dependent proteins, six for riboflavin and in revised form 21 February 2013 uptake and transformation into the active coenzymes FMN and FAD as well as two for the reduction to Available online 15 March 2013 the dihydroflavin form. Flavoproteins utilize either FMN (16%) or FAD (84%) while five human flavoen- zymes have a requirement for both FMN and FAD. The majority of flavin-dependent enzymes catalyze Keywords: oxidation–reduction processes in primary metabolic pathways such as the citric acid cycle, b-oxidation Coenzyme A and degradation of amino acids. Ten flavoproteins occur as isozymes and assume special functions in Coenzyme Q the human organism. Two thirds of flavin-dependent proteins are associated with disorders caused by Folate Heme allelic variants affecting protein function. Flavin-dependent proteins also play an important role in the Pyridoxal 50-phosphate biosynthesis of other essential cofactors and hormones such as coenzyme A, coenzyme Q, heme, pyri- Steroids doxal 50-phosphate, steroids and thyroxine. Moreover, they are important for the regulation of folate Thyroxine metabolites by using tetrahydrofolate as cosubstrate in choline degradation, reduction of N-5.10-meth- Vitamins ylenetetrahydrofolate to N-5-methyltetrahydrofolate and maintenance of the catalytically competent form of methionine synthase.
    [Show full text]
  • The Role of Intermembrane Space Redox Factors in Glutathione Metabolism and Intracellular Redox Equilibrium Hatice Kubra Ozer University of South Carolina
    University of South Carolina Scholar Commons Theses and Dissertations 2015 The Role of Intermembrane Space Redox Factors In Glutathione Metabolism And Intracellular Redox Equilibrium Hatice Kubra Ozer University of South carolina Follow this and additional works at: https://scholarcommons.sc.edu/etd Part of the Chemistry Commons Recommended Citation Ozer, H. K.(2015). The Role of Intermembrane Space Redox Factors In Glutathione Metabolism And Intracellular Redox Equilibrium. (Doctoral dissertation). Retrieved from https://scholarcommons.sc.edu/etd/3702 This Open Access Dissertation is brought to you by Scholar Commons. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of Scholar Commons. For more information, please contact [email protected]. THE ROLE OF INTERMEMBRANE SPACE REDOX FACTORS IN GLUTATHIONE METABOLISM AND INTRACELLULAR REDOX EQUILIBRIUM by Hatice Kubra Ozer Bachelor of Science Uludag University, 2004 Master of Food Science and Nutrition Clemson University, 2010 Submitted in Partial Fulfillment of the Requirements For the Degree of Doctor of Philosophy in Chemistry College of Arts and Sciences University of South Carolina 2015 Accepted by: Caryn E. Outten, Major Professor F. Wayne Outten, Committee Chair Erin Connolly, Committee Member Andrew B. Greytak, Committee Member Lacy K. Ford, Senior Vice Provost and Dean of Graduate Studies © Copyright by Hatice Kubra Ozer, 2015 All Rights Reserved. ii ACKNOWLEDGEMENTS First, I would like to thank my advisor, Dr. Caryn E. Outten for her patience, guidance, expertise, and confidence in me to complete the work contained herein. She has been an excellent mentor during my graduate program. She is also the only person beside myself who is guaranteed to have read every word of this manuscript and to review every presentations in the past and her insight was irreplaceable.
    [Show full text]
  • Comparative Transcriptome Analysis of Waterlogging-Sensitive
    Article Comparative Transcriptome Analysis of Waterlogging-Sensitive and Tolerant Zombi Pea (Vigna Vexillata) Reveals Energy Conservation and Root Plasticity Controlling Waterlogging Tolerance Pimprapai Butsayawarapat 1, Piyada Juntawong 1,2,3*, Ornusa Khamsuk 4 and Prakit Somta 5 1 Department of Genetics, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand 2 Center for Advanced Studies in Tropical Natural Resources, National Research University -Kasetsart University, Bangkok 10900, Thailand 3 Omics Center for Agriculture, Bioresources, Food and Health, Kasetsart University (OmiKU), Bangkok 10900, Thailand 4 Department of Botany, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand 5 Department of Agronomy, Faculty of Agriculture at Kamphaeng Saen, Kasetsart University, Nakhon Pathom 73140, Thailand *Correspondence: [email protected]; Tel.: +66-02-562-5555 Received: 22 June 2019; Accepted: 31 July 2019; Published: 2 August 2019 Abstract: Vigna vexillata (zombi pea) is an underutilized legume crop considered to be a potential gene source in breeding for abiotic stress tolerance. This study focuses on the molecular characterization of mechanisms controlling waterlogging tolerance using two zombi pea varieties with contrasting waterlogging tolerance. Morphological examination revealed that in contrast to the sensitive variety, the tolerant variety was able to grow, maintain chlorophyll, form lateral roots, and develop aerenchyma in hypocotyl and taproots under waterlogging. To find the mechanism controlling waterlogging tolerance in zombi pea, comparative transcriptome analysis was performed using roots subjected to short-term waterlogging. Functional analysis indicated that glycolysis and fermentative genes were strongly upregulated in the sensitive variety, but not in the tolerant one. In contrast, the genes involved in auxin-regulated lateral root initiation and formation were expressed only in the tolerant variety.
    [Show full text]