DOCSLIB.ORG

Regulation of S-Adenosylmethionine Synthetase Genes in Amoebae by Bacterial Endosymbionts

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 8-2003 Regulation of S-adenosylmethionine synthetase genes in amoebae by bacterial endosymbionts Taeck-Joong Jeon Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Recommended Citation Jeon, Taeck-Joong, "Regulation of S-adenosylmethionine synthetase genes in amoebae by bacterial endosymbionts. " PhD diss., University of Tennessee, 2003. https://trace.tennessee.edu/utk_graddiss/5141 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Taeck-Joong Jeon entitled "Regulation of S- adenosylmethionine synthetase genes in amoebae by bacterial endosymbionts." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the equirr ements for the degree of Doctor of Philosophy, with a major in Biochemistry and Cellular and Molecular Biology. Kwang W. Jeon, Major Professor We have read this dissertation and recommend its acceptance: Accepted for the Council: Carolyn R. Hodges Vice Provost and Dean of the Graduate School (Original signatures are on file with official studentecor r ds.) To the Graduate Council: I am submitting herewith a dissertation written by Taeck-Joong Jeon entitled "Regulation of S-adenosylmethionine synthetase genes in amoebaeby bacterial endosymbionts." I have examinedthe final paper copy of this dissertation for formand content and recommend that it be accepted in partial fulfillmentof the requirements for the degree of Doctor of Philosophy, with a major in Biochemistry and Cellular and Molecular Biology. We have read this dissertation and recommend its acceptance: Accepted for the Council: Vice Provost and Dean raduate Studies REGULATION OF S-ADENOSYLMETHIONINE SYNTHETASE GENES IN AMOEBAE BY BACTERIAL ENDOSYMBIONTS A Dissertation Presented forthe Doctor of Philosophy Degree The University of Tennessee, Knoxville Taeck-Joong Jeon August 2003 DEDICATION This dissertation is dedicated to my parents Mr. Byung-InJeon and Mrs. Joong-Ok Nam 11.. ACKNOWLEDGEMENTS I am most gratefulto my major professor, Dr. Kwang W. Jeon who has been a fatheror uncle figure in these past five years. Without his patience, support, and encouragement, I would not be where I stand now. He will remain in my mind as a person of patience, generosity, and care. I also thankother members of my dissertation committee, Drs. BarryBruce, Ranjan Ganguly, Bruce D. McKee, and Albrecht von Arnim for their advice, helpful suggestions, and critical reviews on my research. I wish to express my special gratitude to Drs. Kil-Jae Lee and Tae In Ahn who encouraged and helped me to continue my graduate study in this laboratory andgave me helpful suggestions from far away. I also thank Dr. Sang Wook Oh for his guidance in taking care ofamoebae and lab in the beginning of my graduate work and Dr. Siuk Yoo for his help in my study. This study was supported by Dr. Jeon's grant from the National Science Foundation. I am also gratefulto the Department of Biochemistry and Cellular and Molecular Biology at the University of Tennessee, Knoxville, for financialsupport in the form of Graduate Teaching Assistantship. I wish to express my sincere gratitudeto my parents, Mr. Byung-In Jeon and Mrs. Joong-Ok Nam, and all my family members for their everlasting love and encouragement. Finally, I express my deepest gratitudeto my wife, Hyona Baek. Without her sacrifice, support, and love, none of this would have been possible. I also thank my son, Jonghee, who has always pleased me. 111... ABSTRACT The xD strain of Amoeba proteus that arose fromthe D strain by spontaneous infectionof X-bacteria is now dependenton X-bacteria forsurvival. The S­ adenosylmethionine synthetase (SAMS) is the enzymethat catalyzes the synthesis of S­ adenosylmethionine (SAM), a major methyl donor in cells. As a result of harboring obligatory bacterial endosymbionts, xD amoebae do not transcribe the sams gene and no longer produce their own SAMS. When symbiont-freeD amoebae are infectedwith symbionts (X-bacteria), the amountof amoebaSAMS decreases to a negligible level within fourweeks, but about 4 7% of the SAMS activity, which apparently comes from another source,is still detected. Therefore,it was postulated that X-bacteria suppressed the expression of amoeba's sams and in turnprovided the enzymeof SAM for their hosts, forcinghost amoebaeto become dependent on symbionts themselves. As a partof my work to elucidate the mechanism forthe development of mutual dependence between symbionts andhosts, firstthe sams genes of amoebaeand X­ bacteria were cloned andcharacterized (PART II}. The previously reported sams gene of amoebaeturned out to be an isoform,so now we call the gene sams 1. The open reading frameof the amoeba'ssamsl gene has 1,281 nucleotides, encoding SAMS of 426 amino acids with a mass of 48 kDa andpl of 6.5. The 5'-flankingregion of amoeba samsl contains consensus-binding sites for several transcription factorsthat are related to the regulation of sams genes in E. coli andyeast. The open reading frameof X-bacteria sams is 1,146 nucleotides long, encoding SAMS of 381 amino acids with a mass of 41 kDa and pl of 6.0. The X-bacteria SAMS has 45% sequence identity with that of A. proteus. Next I tested if symbionts supplied SAMS or SAM to host xD amoebaeby localizing X-bacteria SAMS in xD amoebaeand measuring SAMS activities in D and xD amoebae (PART Ill). The results show that amoebaehave a second sams (sams2) gene, encoding 390 amino acids and that the SAMS activity foundin xD amoebae comes from SAMS2 not from the endosymbionts. Interestingly, the expression of two amoeba sams genes was switched from samsl to sams2 by infectionwith X-bacteria, raising a possibility that the switch in the expression of sams genes by bacteria plays a role in the IV development of symbiosis and the host-pathogen interactions. This is the firstreport showing the switch in the expression of host sams genes by infecting bacteria. In PART IV, the analysis forDNA adenine methylation of samsl shows that the samsl gene is methylated at an internaladenine residue ofGATC site in xD amoebae whereas no methylation occurs in D amoebae. This result implies that the modification might be the reason for the suppression of sams 1 in xD amoebae. The methylation of cytosine residue in CpG sites is the most common modificationin eukaryotes. However, it appears that the methylation of cytosine residues is not responsible for the inactivation of samsl in xD amoebae. DNA analysis shows that adenine residues in X-bacteria sams are also methylated, indicating Legionella-like X-bacteria belong to Dam methylase­ positive strains. In addition, it appears that SAM and methionine act as a negative regulator for the expression of samsl whereas the expression of sams2 is not affectedin amoebae. After the removal ofX-bacteria fromxD amoebae, the samsl gene was reactivated and sams2 was down-regulated. The results are reversed in the expression of sams genes when amoebae are infected with X-bacteria. This is the first report to show that a specific eukaryotic gene is modified by DNA adenine methylation. V TABLE OF CONTENTS PART PAGE I. GENERAL INTRODUCTION AND OVERVIEW ----------------------------- 1 1) Amoeba/X-bacteria Symbiosis --------------------------------------------------------- 2 2) S-adenosylmethionine synthetase (SAMS) ------------------------------------------- 4 3) SpecificAims ----------------------------------------------------------------------------- 7 References --------------------------------------------------------------------------------- 8 II. CHARACTERIZATION OF SAMS GENES OF AMOEBA PROTEUS AND THE ENDOSYMBIOTIC X-BACTERIA ---------------------------------------- 11 1) Abstract ---------------------------------------------------------------------------------- 12 2) Introduction ------------------------------------------------------------------------------ 13 3) Materials and Methods ----------------------------------------------------------------- 15 4) Results ------------------------------------------------------------------------------------ 21 5) Discussion ------------------------------------------------------------------------------- 25 References -------------------------------------------------------------------------------- 29 Appendix --------------------------------------------------------------------------------- 3 2 III. GENE SWITCHING IN AMOEBA PROTEUS CAUSED BY ENDOSYMBIOTI C BACTERIA -------------------------------------------------- 42 1) Abstract ---------------------------------------------------------------------------------- 43 2) Introduction ----------------------------------------------------------------------------- 44 3) Materials and Methods ---------------------------------------------------------------- 46 4) Results ------------------------------------------------------------------------------------ 52 5) Discussion ------------------------------------------------------------------------------- 57 References ------------------------------------------------------------------------------- 62 Appendix ---------------------------------------------------------------------------------
Recommended publications
  • Characterization of L-Serine Deaminases, Sdaa (PA2448) and Sdab 2 (PA5379), and Their Potential Role in Pseudomonas Aeruginosa 3 Pathogenesis 4 5 Sixto M

    Characterization of L-Serine Deaminases, Sdaa (PA2448) and Sdab 2 (PA5379), and Their Potential Role in Pseudomonas Aeruginosa 3 Pathogenesis 4 5 Sixto M

    bioRxiv preprint doi: https://doi.org/10.1101/394957; this version posted August 20, 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. 1 Characterization of L-serine deaminases, SdaA (PA2448) and SdaB 2 (PA5379), and their potential role in Pseudomonas aeruginosa 3 pathogenesis 4 5 Sixto M. Leal1,6, Elaine Newman2 and Kalai Mathee1,3,4,5 * 6 7 Author affiliations: 8 9 1Department of Biological Sciences, College of Arts Sciences and 10 Education, Florida International University, Miami, United States of 11 America 12 2Department of Biological Sciences, Concordia University, Montreal, 13 Canada 14 3Department of Molecular Microbiology and Infectious Diseases, Herbert 15 Wertheim College of Medicine, Florida International University, Miami, 16 United States of America 17 4Biomolecular Sciences Institute, Florida International University, Miami, 18 United States of America 19 20 Present address: 21 22 5Department of Human and Molecular Genetics, Herbert Wertheim 23 College of Medicine, Florida International University, Miami, United States 24 of America 25 6Case Western Reserve University, United States of America 26 27 28 *Correspondance: Kalai Mathee, MS, PhD, 29 [email protected] 30 31 Telephone : 1-305-348-0628 32 33 Keywords: Serine Catabolism, Central Metabolism, TCA Cycle, Pyruvate, 34 Leucine Responsive Regulatory Protein (LRP), One Carbon Metabolism 35 Running title: P. aeruginosa L-serine deaminases 36 Subject category: Pathogenicity and Virulence/Host Response 37 1 bioRxiv preprint doi: https://doi.org/10.1101/394957; this version posted August 20, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.
  • Methionine Synthase Supports Tumor Tetrahydrofolate Pools

    Methionine Synthase Supports Tumor Tetrahydrofolate Pools

    bioRxiv preprint doi: https://doi.org/10.1101/2020.09.05.284521; this version posted September 7, 2020. 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. Methionine synthase supports tumor tetrahydrofolate pools Joshua Z. Wang1,2,#, Jonathan M. Ghergurovich1,3,#, Lifeng Yang1,2, and Joshua D. Rabinowitz1,2,* 1 Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, New Jersey, USA 2 Department of Chemistry, Princeton University, Princeton, New Jersey, USA 3 Department of Molecular Biology, Princeton University, Princeton, New Jersey, USA # These authors contributed equally to this work. *Corresponding author: Joshua Rabinowitz Department of Chemistry and the Lewis-Sigler Institute for Integrative Genomics, Princeton University, Washington Rd, Princeton, NJ 08544, USA Phone: (609) 258-8985; e-mail: [email protected] Conflict of Interest Disclosure: J.D.R. is a paid advisor and stockholder in Kadmon Pharmaceuticals, L.E.A.F. Pharmaceuticals, and Rafael Pharmaceuticals; a paid consultant of Pfizer; a founder, director, and stockholder of Farber Partners and Serien Therapeutics. JDR and JMG are inventors of patents in the area of folate metabolism held by Princeton University. 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.09.05.284521; this version posted September 7, 2020. 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 Mammalian cells require activated folates to generate nucleotides for growth and division. The most abundant circulating folate species is 5-methyl tetrahydrofolate (5-methyl- THF), which is used to synthesize methionine from homocysteine via the cobalamin-dependent enzyme methionine synthase (MTR).
  • Defining Sources of Nutrient Limitation for Tumors By

    Defining Sources of Nutrient Limitation for Tumors By

    Defining sources of nutrient limitation for tumors by Mark Robert Sullivan B.S. Molecular Biology and Chemistry University of Pittsburgh (2013) Submitted to the Department of Biology in Partial Fulfillment of the Requirements for the Degree of DOCTOR OF PHILOSOPHY at the MASSACHUSETTS INSTITUTE OF TECHNOLOGY June 2019 © 2019 Mark R. Sullivan. All rights reserved. The author hereby grants to MIT permission to reproduce and to distribute publicly paper and electronic copies of this thesis document in whole or in part in any medium now known or hereafter created. Signature of Author.......................................................................................................................... Department of Biology April 30, 2019 Certified by ...................................................................................................................................... Matthew G. Vander Heiden Associate Professor of Biology Thesis Supervisor Accepted by...................................................................................................................................... Amy E. Keating Professor of Biology Co-Director, Biology Graduate Committee 1 2 Defining sources of nutrient limitation for tumors by Mark Robert Sullivan Submitted to the Department of Biology on April 30, 2019 in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy in Biology ABSTRACT Tumor growth requires that cancer cells accumulate sufficient biomass to grow and divide. To accomplish this, tumor cells must acquire
  • Production of L-Asparaginase II by Escherichia Coli HOWARD CEDAR and JAMES H

    Production of L-Asparaginase II by Escherichia Coli HOWARD CEDAR and JAMES H

    JOURNAL OF BACTERIOLOGY, Dec. 1968, p. 2043-2048 Vol. 96, No. 6 Copyright @ 1968 American Society for Microbiology Printed in U.S.A. Production of L-Asparaginase II by Escherichia coli HOWARD CEDAR AND JAMES H. SCHWARTZ Department of Microbiology, New York University School ofMedicine, New York, New York 10016 Received for publication 30 July 1968 L-Asparaginase II was synthesized at constant rates by Escherichia coli under anaerobic conditions. The enzyme was produced optimally by bacteria grown between pH 7 and 8 at 37 C. Although some enzyme was formed aerobically, be- tween 100 and 1,000 times more asparaginase II was produced during anaerobic growth in media enriched with high concentrations of a variety of amino acids. Bacteria grown under these conditions should provide a rich starting material for the large-scale production of the enzyme. No single amino acid specifically induced the synthesis of the asparaginase, nor did L-asparagine, even when it was used as the only source of nitrogen. The enzyme was produced at lower rates in the presence of sugars; glucose was the most inhibitory. Deamidation of L-asparagine by extracts of the conditions which control the production of Escherichia coli was first reported in 1957 by asparaginase II. Tsuji (28). E. coli was later shown to produce two distinct asparaginases (L-asparagine amido- MATERIALS AND METHODS hydrolase, EC 3.5.1 .1) which differ in a number For most of the experiments, we used E. coli K-12 of properties, perhaps most significantly in wild type. We also used strain 22-64, which lacks their markedly different affinities for asparagine citrate synthase (10), and strain 309-1, which lacks (5, 24, 27).
  • Involvements of Hyperhomocysteinemia in Neurological Disorders

    Involvements of Hyperhomocysteinemia in Neurological Disorders

    H OH metabolites OH Review Involvements of Hyperhomocysteinemia in Neurological Disorders Marika Cordaro 1,† , Rosalba Siracusa 2,† , Roberta Fusco 2 , Salvatore Cuzzocrea 2,3,* , Rosanna Di Paola 2,* and Daniela Impellizzeri 2 1 Department of Biomedical, Dental and Morphological and Functional Imaging, University of Messina, Via Consolare Valeria, 98125 Messina, Italy; [email protected] 2 Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy; [email protected] (R.S.); [email protected] (R.F.); [email protected] (D.I.) 3 Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, Saint Louis, MO 63104, USA * Correspondence: [email protected] (S.C.); [email protected] (R.D.P.); Tel.: +39-090-6765208 (S.C. & R.D.P.) † The authors equally contributed to the review. Abstract: Homocysteine (HCY), a physiological amino acid formed when proteins break down, leads to a pathological condition called hyperhomocysteinemia (HHCY), when it is over a definite limit. It is well known that an increase in HCY levels in blood, can contribute to arterial damage and several cardiovascular disease, but the knowledge about the relationship between HCY and brain disorders is very poor. Recent studies demonstrated that an alteration in HCY metabolism or a deficiency in folate or vitamin B12 can cause altered methylation and/or redox potentials, that leads to a modification on calcium influx in cells, or into an accumulation in amyloid and/or tau protein involving a cascade of events that culminate in apoptosis, and, in the worst conditions, neuronal death. The present review will thus summarize how much is known about the possible role of HHCY in neurodegenerative disease.
  • Introduction to Proteins and Amino Acids Introduction

    Introduction to Proteins and Amino Acids Introduction

    Introduction to Proteins and Amino Acids Introduction • Twenty percent of the human body is made up of proteins. Proteins are the large, complex molecules that are critical for normal functioning of cells. • They are essential for the structure, function, and regulation of the body’s tissues and organs. • Proteins are made up of smaller units called amino acids, which are building blocks of proteins. They are attached to one another by peptide bonds forming a long chain of proteins. Amino acid structure and its classification • An amino acid contains both a carboxylic group and an amino group. Amino acids that have an amino group bonded directly to the alpha-carbon are referred to as alpha amino acids. • Every alpha amino acid has a carbon atom, called an alpha carbon, Cα ; bonded to a carboxylic acid, –COOH group; an amino, –NH2 group; a hydrogen atom; and an R group that is unique for every amino acid. Classification of amino acids • There are 20 amino acids. Based on the nature of their ‘R’ group, they are classified based on their polarity as: Classification based on essentiality: Essential amino acids are the amino acids which you need through your diet because your body cannot make them. Whereas non essential amino acids are the amino acids which are not an essential part of your diet because they can be synthesized by your body. Essential Non essential Histidine Alanine Isoleucine Arginine Leucine Aspargine Methionine Aspartate Phenyl alanine Cystine Threonine Glutamic acid Tryptophan Glycine Valine Ornithine Proline Serine Tyrosine Peptide bonds • Amino acids are linked together by ‘amide groups’ called peptide bonds.
  • Isolation and Nucleotide Sequence of the Cdna for Rat Liver Serine

    Isolation and Nucleotide Sequence of the Cdna for Rat Liver Serine

    Proc. Natl. Acad. Sci. USA Vol. 85, pp. 5809-5813, August 1988 Biochemistry Isolation and nucleotide sequence of the cDNA for rat liver serine dehydratase mRNA and structures of the 5' and 3' flanking regions of the serine dehydratase gene (threonine dehydratase/hormonal regulation/consensus sequences) HIROFUMI OGAWA*t, DUNCAN A. MILLER*, TRACY DUNN*, YEU SU*, JAMES M. BURCHAMt, CARL PERAINOt, MOTOJI FUJIOKAt, KAY BABCOCK*, AND HENRY C. PITOT*§ *McArdle Laboratory for Cancer Research, The Medical School, University of Wisconsin, Madison, WI 53706; tDepartment of Biochemistry, Toyama Medical and Pharmaceutical University, Faculty of Medicine, Sugitani, Toyama 930-01, Japan; and tDivision of Biological and Medical Research, Argonne National Laboratory, Argonne, IL 60439 Communicated by Van R. Potter, April 15, 1988 (received for review December 29, 1987) ABSTRACT Rat serine dehydratase cDNA clones were determination of the exact size of DNA complementary to isolated from a Agtll cDNA library on the basis of their serine dehydratase mRNA was made by S1 nuclease and reactivity with monospecific immunoglobulin to the purified sequencing of genomic clones of the regions flanking the enzyme. Using the cDNA insert from a clone that encoded the gene. serine dehydratase subunit as a probe, additional clones were isolated from the same library by plaque hybridization. Nucle- otide sequence analysis of the largest clone obtained showed MATERIALS AND METHODS that it has 1444 base pairs with an open reading frame consisting of 1089 base pairs. The deduced amino acid sequence cDNA Cloning. A rat liver cDNA library constructed in contained sequences of several portions of the serine dehydra- Agtll phage (13) was screened for antibody-reactive plaques tase protein, as determined by Edman degradation.
  • Amino Acid Chemistry

    Amino Acid Chemistry

    Handout 4 Amino Acid and Protein Chemistry ANSC 619 PHYSIOLOGICAL CHEMISTRY OF LIVESTOCK SPECIES Amino Acid Chemistry I. Chemistry of amino acids A. General amino acid structure + HN3- 1. All amino acids are carboxylic acids, i.e., they have a –COOH group at the #1 carbon. 2. All amino acids contain an amino group at the #2 carbon (may amino acids have a second amino group). 3. All amino acids are zwitterions – they contain both positive and negative charges at physiological pH. II. Essential and nonessential amino acids A. Nonessential amino acids: can make the carbon skeleton 1. From glycolysis. 2. From the TCA cycle. B. Nonessential if it can be made from an essential amino acid. 1. Amino acid "sparing". 2. May still be essential under some conditions. C. Essential amino acids 1. Branched chain amino acids (isoleucine, leucine and valine) 2. Lysine 3. Methionine 4. Phenyalanine 5. Threonine 6. Tryptophan 1 Handout 4 Amino Acid and Protein Chemistry D. Essential during rapid growth or for optimal health 1. Arginine 2. Histidine E. Nonessential amino acids 1. Alanine (from pyruvate) 2. Aspartate, asparagine (from oxaloacetate) 3. Cysteine (from serine and methionine) 4. Glutamate, glutamine (from α-ketoglutarate) 5. Glycine (from serine) 6. Proline (from glutamate) 7. Serine (from 3-phosphoglycerate) 8. Tyrosine (from phenylalanine) E. Nonessential and not required for protein synthesis 1. Hydroxyproline (made postranslationally from proline) 2. Hydroxylysine (made postranslationally from lysine) III. Acidic, basic, polar, and hydrophobic amino acids A. Acidic amino acids: amino acids that can donate a hydrogen ion (proton) and thereby decrease pH in an aqueous solution 1.
  • Recycling of Vitamin B12 and NAD+ Within the Pdu Microcompartment of Salmonella Enterica Shouqiang Cheng Iowa State University

    Recycling of Vitamin B12 and NAD+ Within the Pdu Microcompartment of Salmonella Enterica Shouqiang Cheng Iowa State University

    Iowa State University Capstones, Theses and Graduate Theses and Dissertations Dissertations 2010 Recycling of vitamin B12 and NAD+ within the Pdu microcompartment of Salmonella enterica Shouqiang Cheng Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/etd Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Cheng, Shouqiang, "Recycling of vitamin B12 and NAD+ within the Pdu microcompartment of Salmonella enterica" (2010). Graduate Theses and Dissertations. 11713. https://lib.dr.iastate.edu/etd/11713 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 Graduate Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. + Recycling of vitamin B12 and NAD within the Pdu microcompartment of Salmonella enterica by Shouqiang Cheng A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Biochemistry Program of Study Committee: Thomas A. Bobik, Major Professor Alan DiSpirito Basil Nikolau Reuben Peters Gregory J. Phillips Iowa State University Ames, Iowa 2010 Copyright © Shouqiang Cheng, 2010. All rights reserved. ii Table of contents Abstract.............................................................................................................................
  • Polymorphisms in Methionine Synthase, Methionine Synthase Reductase and Serine Hydroxymethyltransferase, Folate and Alcohol Intake, and Colon Cancer Risk Susan E

    Polymorphisms in Methionine Synthase, Methionine Synthase Reductase and Serine Hydroxymethyltransferase, Folate and Alcohol Intake, and Colon Cancer Risk Susan E

    University of South Carolina Scholar Commons Faculty Publications Epidemiology and Biostatistics 2008 Polymorphisms in Methionine Synthase, Methionine Synthase Reductase and Serine Hydroxymethyltransferase, Folate and Alcohol Intake, and Colon Cancer Risk Susan E. Steck University of South Carolina - Columbia, [email protected] Temitope O. Keku Lesley M. Butler Joseph Galanko Beri Massa See next page for additional authors Follow this and additional works at: https://scholarcommons.sc.edu/ sph_epidemiology_biostatistics_facpub Part of the Public Health Commons Publication Info Postprint version. Published in Journal of Nutrigenetics and Nutrigenomics, Volume 1, Issue 4, 2008, pages 196-204. Steck, S. E., Keku, T., Butler, L. M., Galanko, J., Massa, B., Millikan, R. C., & Sandler, R. S. (2008). Polymorphisms in methionine synthase, methionine synthase reductase and serine hydroxymethyltransferase, folate and alcohol intake, and colon cancer risk. Journal of Nutrigenetics and Nutrigenomics, 1(4), 196-204. DOI: 10.1159/000136651 © Journal of Nutrigenetics and Nutrigenomics, 2008, Karger http://content.karger.com/produktedb/produkte.asp?DOI=10.1159/000136651 This Article is brought to you by the Epidemiology and Biostatistics at Scholar Commons. It has been accepted for inclusion in Faculty Publications by an authorized administrator of Scholar Commons. For more information, please contact [email protected]. Author(s) Susan E. Steck, Temitope O. Keku, Lesley M. Butler, Joseph Galanko, Beri Massa, Robert C. Millikan, and Robert S. Sandler This article is available at Scholar Commons: https://scholarcommons.sc.edu/sph_epidemiology_biostatistics_facpub/303 NIH Public Access Author Manuscript J Nutrigenet Nutrigenomics. Author manuscript; available in PMC 2009 October 7. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: J Nutrigenet Nutrigenomics.
  • Formate Metabolism in Health and Disease

    Formate Metabolism in Health and Disease

    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Enlighten Review Formate metabolism in health and disease Matthias Pietzke 1, Johannes Meiser 2, Alexei Vazquez 1,3,* ABSTRACT Background: Formate is a one-carbon molecule at the crossroad between cellular and whole body metabolism, between host and microbiome metabolism, and between nutrition and toxicology. This centrality confers formate with a key role in human physiology and disease that is currently unappreciated. Scope of review: Here we review the scientific literature on formate metabolism, highlighting cellular pathways, whole body metabolism, and interactions with the diet and the gut microbiome. We will discuss the relevance of formate metabolism in the context of embryonic development, cancer, obesity, immunometabolism, and neurodegeneration. Major conclusions: We will conclude with an outlook of some open questions bringing formate metabolism into the spotlight. Ó 2019 The Authors. Published by Elsevier GmbH. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). Keywords Formate metabolism; One-carbon-metabolism; Cancer; Immune system; Neurodegeneration; Obesity 1. INTRODUCTION product of anaerobic fermentation of some bacteria species popu- lating the gut microbiome [7]. The formate generated by the gut Formic acid (HCOOH) was first isolated from distillation of ant bodies, bacteria can enter the circulation, adding to the endogenous pool of and it was subsequently named using the Latin word for ant, formica formate or being used as substrate for the growth of other bacteria [1]. Ants and other insects accumulate formic acid in secretory with aerobic metabolism [8].
  • Genome, Proteome and Physiology of the Thermophilic Bacterium Anoxybacillus Flavithermus

    Genome, Proteome and Physiology of the Thermophilic Bacterium Anoxybacillus Flavithermus

    Open Access Research2008SawetVolume al. 9, Issue 11, Article R161 Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1 Jimmy H Saw¤*‡‡, Bruce W Mountain¤†, Lu Feng¤‡§¶, Marina V Omelchenko¤¥, Shaobin Hou¤#, Jennifer A Saito*, Matthew B Stott†, Dan Li‡§¶, Guang Zhao‡§¶, Junli Wu‡§¶, Michael Y Galperin¥, Eugene V Koonin¥, Kira S Makarova¥, Yuri I Wolf¥, Daniel J Rigden**, Peter F Dunfield††, Lei Wang‡§¶ and Maqsudul Alam*# Addresses: *Department of Microbiology, University of Hawai'i, 2538 The Mall, Honolulu, HI 96822, USA. †GNS Science, Extremophile Research Group, 3352 Taupo, New Zealand. ‡TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin 300457, PR China. §Tianjin Research Center for Functional Genomics and Biochip, Tianjin 300457, PR China. ¶Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin 300457, PR China. ¥National Center for Biotechnology Information, NLM, National Institutes of Health, Bethesda, MD 20894, USA. #Advance Studies in Genomics, Proteomics and Bioinformatics, College of Natural Sciences, University of Hawai'i, Honolulu, HI 96822, USA. **School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK. ††Department of Biological Sciences, University of Calgary, 2500 University Dr. NW, Calgary, Alberta T2N 1N4, Canada. ‡‡Current address: Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. ¤ These authors contributed equally to this work. Correspondence: Lei Wang. Email: [email protected]. Maqsudul Alam. Email: [email protected] Published: 17 November 2008 Received: 12 June 2008 Revised: 8 October 2008 Genome Biology 2008, 9:R161 (doi:10.1186/gb-2008-9-11-r161) Accepted: 17 November 2008 The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2008/9/11/R161 © 2008 Saw et al.; licensee BioMed Central Ltd.