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Structural Insights Into Histone Modifying Enzymes
Wayne State University Wayne State University Theses January 2019 Structural Insights Into Histone Modifying Enzymes Shruti Amle Wayne State University, [email protected] Follow this and additional works at: https://digitalcommons.wayne.edu/oa_theses Part of the Biochemistry Commons, and the Molecular Biology Commons Recommended Citation Amle, Shruti, "Structural Insights Into Histone Modifying Enzymes" (2019). Wayne State University Theses. 693. https://digitalcommons.wayne.edu/oa_theses/693 This Open Access Embargo is brought to you for free and open access by DigitalCommons@WayneState. It has been accepted for inclusion in Wayne State University Theses by an authorized administrator of DigitalCommons@WayneState. STRUCTURAL INSIGHTS INTO HISTONE MODIFYING ENZYMES by SHRUTI AMLE THESIS Submitted to the Graduate School of Wayne State University, Detroit, Michigan in partial fulfillment of the requirements for the degree of MASTER OF SCIENCE 2019 MAJOR: BIOCHEMISTRY AND MOLECULAR BIOLOGY Approved By: _________________________________________ Advisor Date _________________________________________ _________________________________________ _________________________________________ i ACKNOWLEDGEMENTS Writing this thesis has been extremely captivating and gratifying. I take this opportunity to express my deep and sincere acknowledgements to the number of people for extending their generous support and unstinted help during my entire study. Firstly, I would like to express my respectful regards and deep sense of gratitude to my advisor, Dr. Zhe Yang. I am extremely honored to study and work under his guidance. His vision, ideals, timely motivation and immense knowledge had a deep influence on my entire journey of this career. Without his understanding and support, it would not have been possible to complete this research successfully. I also owe my special thanks to my committee members: Dr. -
Structural Properties of the Nickel Ions in Urease: Novel Insights Into the Catalytic and Inhibition Mechanisms
Coordination Chemistry Reviews 190–192 (1999) 331–355 www.elsevier.com/locate/ccr Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms Stefano Ciurli a,*, Stefano Benini b, Wojciech R. Rypniewski b, Keith S. Wilson c, Silvia Miletti a, Stefano Mangani d a Institute of Agricultural Chemistry, Uni6ersity of Bologna, Viale Berti Pichat 10, I-40127 Bologna, Italy b European Molecular Biology Laboratory, c/o DESY, Notkestraße 85, D-22603 Hamburg, Germany c Department of Chemistry, Uni6ersity of York, Heslington, York YO15DD, UK d Department of Chemistry, Uni6ersity of Siena, Pian dei Mantellini 44, I-53100 Siena, Italy Accepted 13 March 1999 Contents Abstract.................................................... 331 1. Biological background ......................................... 332 2. Spectroscopic investigations of the urease active site structure .................. 333 3. Crystallographic studies of the native enzyme ............................ 334 4. Crystallographic studies of urease mutants.............................. 341 5. Crystallographic studies of urease–inhibitor complexes ...................... 345 6. Crystallographic study of a transition state analogue bound to urease.............. 348 7. A novel proposal for the urease mechanism ............................. 350 References .................................................. 353 Abstract This work provides a comprehensive critical summary of urease spectroscopy, crystallogra- phy, inhibitor binding, and site-directed -
Discovery of an Alternate Metabolic Pathway for Urea Synthesis in Adult Aedes Aegypti Mosquitoes
Discovery of an alternate metabolic pathway for urea synthesis in adult Aedes aegypti mosquitoes Patricia Y. Scaraffia*†‡, Guanhong Tan§, Jun Isoe*†, Vicki H. Wysocki*§, Michael A. Wells*†, and Roger L. Miesfeld*† Departments of §Chemistry and *Biochemistry and Molecular Biophysics and †Center for Insect Science, University of Arizona, Tucson, AZ 85721-0088 Edited by Anthony A. James, University of California, Irvine, CA, and approved December 4, 2007 (received for review August 27, 2007) We demonstrate the presence of an alternate metabolic pathway We previously reported that mosquitoes dispose of toxic for urea synthesis in Aedes aegypti mosquitoes that converts uric ammonia through glutamine (Gln) and proline (Pro) synthesis, acid to urea via an amphibian-like uricolytic pathway. For these along with excretion of ammonia, uric acid, and urea (20). By studies, female mosquitoes were fed a sucrose solution containing using labeled isotopes and mass spectrometry techniques (21), 15 15 15 15 15 NH4Cl, [5- N]-glutamine, [ N]-proline, allantoin, or allantoic we have recently determined how the N from NH4Cl is acid. At 24 h after feeding, the feces were collected and analyzed incorporated into the amide side chain of Gln, and then into Pro, in a mass spectrometer. Specific enzyme inhibitors confirmed that in Ae. aegypti (22). In the present article we demonstrate that the 15 15 15 mosquitoes incorporate N from NH4Cl into [5- N]-glutamine nitrogen of the amide group of Gln contributes to uric acid and use the 15N of the amide group of glutamine to produce synthesis in mosquitoes and, surprisingly, that uric acid can be 15 labeled uric acid. -
Francisella Tularensis 6/06 Tularemia Is a Commonly Acquired Laboratory Colony Morphology Infection; All Work on Suspect F
Francisella tularensis 6/06 Tularemia is a commonly acquired laboratory Colony Morphology infection; all work on suspect F. tularensis cultures .Aerobic, fastidious, requires cysteine for growth should be performed at minimum under BSL2 .Grows poorly on Blood Agar (BA) conditions with BSL3 practices. .Chocolate Agar (CA): tiny, grey-white, opaque A colonies, 1-2 mm ≥48hr B .Cysteine Heart Agar (CHA): greenish-blue colonies, 2-4 mm ≥48h .Colonies are butyrous and smooth Gram Stain .Tiny, 0.2–0.7 μm pleomorphic, poorly stained gram-negative coccobacilli .Mostly single cells Growth on BA (A) 48 h, (B) 72 h Biochemical/Test Reactions .Oxidase: Negative A B .Catalase: Weak positive .Urease: Negative Additional Information .Can be misidentified as: Haemophilus influenzae, Actinobacillus spp. by automated ID systems .Infective Dose: 10 colony forming units Biosafety Level 3 agent (once Francisella tularensis is . Growth on CA (A) 48 h, (B) 72 h suspected, work should only be done in a certified Class II Biosafety Cabinet) .Transmission: Inhalation, insect bite, contact with tissues or bodily fluids of infected animals .Contagious: No Acceptable Specimen Types .Tissue biopsy .Whole blood: 5-10 ml blood in EDTA, and/or Inoculated blood culture bottle Swab of lesion in transport media . Gram stain Sentinel Laboratory Rule-Out of Francisella tularensis Oxidase Little to no growth on BA >48 h Small, grey-white opaque colonies on CA after ≥48 h at 35/37ºC Positive Weak Negative Positive Catalase Tiny, pleomorphic, faintly stained, gram-negative coccobacilli (red, round, and random) Perform all additional work in a certified Class II Positive Biosafety Cabinet Weak Negative Positive *Oxidase: Negative Urease *Catalase: Weak positive *Urease: Negative *Oxidase, Catalase, and Urease: Appearances of test results are not agent-specific. -
Extended Spectrum Β-Lactamases and Class C Β
F1000Research 2020, 9:774 Last updated: 01 APR 2021 RESEARCH ARTICLE Extended spectrum β-lactamases and class C β-lactamases gene frequency in Pseudomonas aeruginosa isolated from various clinical specimens in Khartoum State, Sudan: a cross sectional study [version 1; peer review: 1 not approved] Dina N. Abdelrahman 1,2, Aya A. Taha2, Mazar M. Dafaallah2, Alaa Abdelgafoor Mohammed3, Abdel Rahim M. El Hussein 1, Ahmed I. Hashim 2, Yousif F. Hamedelnil2, Hisham N. Altayb 4 1Department of Virology, Central Laboratory, Khartoum, Sudan 2Department of Microbiology, College of Medical Laboratory Sciences, Sudan University of Science and Technology, Khartoum, Sudan 3Department of Pharmaceutical Biotechnology, College of Pharmacy, Ahfad University for Women, Omdurman, Khartoum, Sudan 4Biochemistry Department, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia v1 First published: 27 Jul 2020, 9:774 Open Peer Review https://doi.org/10.12688/f1000research.24818.1 Second version: 15 Sep 2020, 9:774 https://doi.org/10.12688/f1000research.24818.2 Reviewer Status Latest published: 01 Apr 2021, 9:774 https://doi.org/10.12688/f1000research.24818.3 Invited Reviewers 1 2 Abstract Background: Pseudomonas aeruginosa is a pathogenic bacterium, version 3 causing nosocomial infections with intrinsic and acquired resistance (revision) mechanisms to a large group of antibiotics, including β-lactams. This 01 Apr 2021 study aimed to determine the susceptibility pattern to selected antibiotics and to index the first reported β-lactamases gene version 2 (extended spectrum β-lactamases (ESBLs) genes and class C β- (revision) report report lactamases genes) frequency in Ps. aeruginosa in Khartoum State, 15 Sep 2020 Sudan. Methods: 121 Ps. -
(12) United States Patent (10) Patent No.: US 9.422,609 B2 Teichberg (45) Date of Patent: Aug
USOO9422609B2 (12) United States Patent (10) Patent No.: US 9.422,609 B2 Teichberg (45) Date of Patent: Aug. 23, 2016 (54) METHODS, COMPOSITIONS AND DEVICES (58) Field of Classification Search FOR MANTAINING CHEMICAL BALANCE CPC ........................ C02F 1/725; C12Y 305/01005 OF CHLORINATED WATER USPC ........................... 210/754; 435/195, 227 231 See application file for complete search history. (75) Inventor: Vivian I. Teichberg, Savyon (IL) (56) References Cited (73) Assignees: Mia Levite, Savyon (IL); Yaar Teichberg, Savyon (IL); Nof Lyle U.S. PATENT DOCUMENTS Teichberg, Savyon (IL) 4,793,935 A * 12/1988 Stillman ............... CO2F 1.5236 21Of727 (*) Notice: Subject to any disclaimer, the term of this 6,673,582 B2 * 1/2004 McTavish ..................... 435/122 patent is extended or adjusted under 35 U.S.C. 154(b) by 1044 days. (Continued) (21) Appl. No.: 12/225.18O FOREIGN PATENT DOCUMENTS y x- - - 9 AU 41971 5, 1979 (22) PCT Filed: Mar. 14, 2007 GB 2025919 1, 1980 (86). PCT No.: PCT/L2007/OOO336 (Continued) S 371 (c)(1) OTHER PUBLICATIONS (2), (4) Date: Sep. 16, 2008 Examiner's Report Dated Oct. 6, 2010 From the Australian Govern (87) PCT Pub. No.: WO2007/107.981 ment, IP Australia Re. Application No. 2007228391. (Continued) PCT Pub. Date: Sep. 27, 2007 (65) Prior Publication Data Primary Examiner — Peter Keyworth (74) Attorney, Agent, or Firm — Browdy and Neimark, US 201OfO270228A1 Oct. 28, 2010 PLLC Related U.S. Application Data (57) ABSTRACT (60) Provisional application No. 60/783,028, filed on Mar. A composition-of-matter for use in water treatment, com 17, 2006. -
Letters to Nature
letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997). -
The Microbiota-Produced N-Formyl Peptide Fmlf Promotes Obesity-Induced Glucose
Page 1 of 230 Diabetes Title: The microbiota-produced N-formyl peptide fMLF promotes obesity-induced glucose intolerance Joshua Wollam1, Matthew Riopel1, Yong-Jiang Xu1,2, Andrew M. F. Johnson1, Jachelle M. Ofrecio1, Wei Ying1, Dalila El Ouarrat1, Luisa S. Chan3, Andrew W. Han3, Nadir A. Mahmood3, Caitlin N. Ryan3, Yun Sok Lee1, Jeramie D. Watrous1,2, Mahendra D. Chordia4, Dongfeng Pan4, Mohit Jain1,2, Jerrold M. Olefsky1 * Affiliations: 1 Division of Endocrinology & Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2 Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 3 Second Genome, Inc., South San Francisco, California, USA. 4 Department of Radiology and Medical Imaging, University of Virginia, Charlottesville, VA, USA. * Correspondence to: 858-534-2230, [email protected] Word Count: 4749 Figures: 6 Supplemental Figures: 11 Supplemental Tables: 5 1 Diabetes Publish Ahead of Print, published online April 22, 2019 Diabetes Page 2 of 230 ABSTRACT The composition of the gastrointestinal (GI) microbiota and associated metabolites changes dramatically with diet and the development of obesity. Although many correlations have been described, specific mechanistic links between these changes and glucose homeostasis remain to be defined. Here we show that blood and intestinal levels of the microbiota-produced N-formyl peptide, formyl-methionyl-leucyl-phenylalanine (fMLF), are elevated in high fat diet (HFD)- induced obese mice. Genetic or pharmacological inhibition of the N-formyl peptide receptor Fpr1 leads to increased insulin levels and improved glucose tolerance, dependent upon glucagon- like peptide-1 (GLP-1). Obese Fpr1-knockout (Fpr1-KO) mice also display an altered microbiome, exemplifying the dynamic relationship between host metabolism and microbiota. -
Download Author Version (PDF)
Food & Function Accepted Manuscript This is an Accepted Manuscript, which has been through the Royal Society of Chemistry peer review process and has been accepted for publication. Accepted Manuscripts are published online shortly after acceptance, before technical editing, formatting and proof reading. Using this free service, authors can make their results available to the community, in citable form, before we publish the edited article. We will replace this Accepted Manuscript with the edited and formatted Advance Article as soon as it is available. You can find more information about Accepted Manuscripts in the Information for Authors. Please note that technical editing may introduce minor changes to the text and/or graphics, which may alter content. The journal’s standard Terms & Conditions and the Ethical guidelines still apply. In no event shall the Royal Society of Chemistry be held responsible for any errors or omissions in this Accepted Manuscript or any consequences arising from the use of any information it contains. www.rsc.org/foodfunction Page 1 of 16 PleaseFood do not & Functionadjust margins Food&Function REVIEW ARTICLE Interactions between acrylamide, microorganisms, and food components – a review. Received 00th January 20xx, a† a a a a Accepted 00th January 20xx A. Duda-Chodak , Ł. Wajda , T. Tarko , P. Sroka , and P. Satora DOI: 10.1039/x0xx00000x Acrylamide (AA) and its metabolites have been recognised as potential carcinogens, but also they can cause other negative symptoms in human or animal organisms so this chemical compounds still attract a lot of attention. Those substances are www.rsc.org/ usually formed during heating asparagine in the presence of compounds that have α-hydroxycarbonyl groups, α,β,γ,δ- diunsaturated carbonyl groups or α-dicarbonyl groups. -
Chemical Transformations Encoded by a Gene Cluster in Streptomyces Coelicolor Containing an Unusual Gtp Cyclohydrolase
Chemical Transformations Encoded by a Streptomyces coelicolor Gene Cluster with an Unusual GTP Cyclohydrolase Item Type text; Electronic Dissertation Authors Spoonamore, James Edward Publisher The University of Arizona. Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. Download date 11/10/2021 06:44:52 Link to Item http://hdl.handle.net/10150/194825 CHEMICAL TRANSFORMATIONS ENCODED BY A GENE CLUSTER IN STREPTOMYCES COELICOLOR CONTAINING AN UNUSUAL GTP CYCLOHYDROLASE by James Edward Spoonamore ______________________________ A Dissertation Submitted to the Faculty of the DEPARTMENT OF BIOCHEMISTRY AND MOLECULAR BIOPHYSICS In Partial Fulfillment of the Requirements For the Degree of DOCTOR OF PHILOSOPHY In the Graduate College THE UNIVERSITY OF ARIZONA 2008 2 THE UNIVERSITY OF ARIZONA GRADUATE COLLEGE As members of the Dissertation Committee, we certify that we have read the dissertation prepared by James Edward Spoonamore entitled Chemical Transformations Encoded by a Gene Cluster in Streptomyces coelicolor Containing an Unusual GTP Cyclohydrolase and recommend that it be accepted as fulfilling the dissertation requirement for the Degree of Doctor of Philosophy _______________________________________________________________________ Date: April 16, 2008 Vahe Bandarian _______________________________________________________________________ -
Supplementary Information
Supplementary information (a) (b) Figure S1. Resistant (a) and sensitive (b) gene scores plotted against subsystems involved in cell regulation. The small circles represent the individual hits and the large circles represent the mean of each subsystem. Each individual score signifies the mean of 12 trials – three biological and four technical. The p-value was calculated as a two-tailed t-test and significance was determined using the Benjamini-Hochberg procedure; false discovery rate was selected to be 0.1. Plots constructed using Pathway Tools, Omics Dashboard. Figure S2. Connectivity map displaying the predicted functional associations between the silver-resistant gene hits; disconnected gene hits not shown. The thicknesses of the lines indicate the degree of confidence prediction for the given interaction, based on fusion, co-occurrence, experimental and co-expression data. Figure produced using STRING (version 10.5) and a medium confidence score (approximate probability) of 0.4. Figure S3. Connectivity map displaying the predicted functional associations between the silver-sensitive gene hits; disconnected gene hits not shown. The thicknesses of the lines indicate the degree of confidence prediction for the given interaction, based on fusion, co-occurrence, experimental and co-expression data. Figure produced using STRING (version 10.5) and a medium confidence score (approximate probability) of 0.4. Figure S4. Metabolic overview of the pathways in Escherichia coli. The pathways involved in silver-resistance are coloured according to respective normalized score. Each individual score represents the mean of 12 trials – three biological and four technical. Amino acid – upward pointing triangle, carbohydrate – square, proteins – diamond, purines – vertical ellipse, cofactor – downward pointing triangle, tRNA – tee, and other – circle. -
PURINE SALVAGE in HELICOBACTER PYLORI by ERICA FRANCESCA MILLER (Under the Direction of Robert J. Maier) ABSTRACT Purines Are Es
PURINE SALVAGE IN HELICOBACTER PYLORI by ERICA FRANCESCA MILLER (Under the Direction of Robert J. Maier) ABSTRACT Purines are essential for all living cells. This fact is reflected in the high degree of pathway conservation for purine metabolism across all domains of life. The availability of purines within a mammalian host is thought to be a limiting factor for infection, as demonstrated by the importance of purine synthesis and salvage genes among many bacterial pathogens. Helicobacter pylori, a primary causative agent of peptic ulcers and gastric cancers, colonizes a niche that is otherwise uninhabited by bacteria: the surface of the human gastric epithelium. Despite many studies over the past 30 years that have addressed virulence mechanisms such as acid resistance, little knowledge exists regarding this organism’s purine metabolism. To fill this gap in knowledge, we asked whether H. pylori can carry out de novo purine biosynthesis, and whether its purine salvage network is complete. Based on genomic data from the fully sequenced H. pylori genomes, we combined mutant analysis with physiological studies to determine that H. pylori, by necessity, must acquire purines from its human host. Furthermore, we found the purine salvage network to be complete, allowing this organism to use any single purine nucleobase or nucleoside for growth. In the process of elucidating these pathways, we discovered a nucleoside transporter in H. pylori that, in contrast to the biochemically- characterized homolog NupC, aids in uptake of purine rather than pyrimidine nucleosides into the cell. Lastly, we investigated an apparent pathway gap in the genome annotation—that of adenine degradation—and in doing so uncovered a new family of adenosine deaminase that lacks sequence homology with all other adenosine deaminases studied to date.