2010 Physical Biosciences Research Meeting

Total Page:16

File Type:pdf, Size:1020Kb

2010 Physical Biosciences Research Meeting 2010 Physical Biosciences Research Meeting Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Office of Basic Energy Sciences Chemical Sciences, Geosciences & Biosciences Division 2010 Physical Biosciences Research Meeting Program and Abstracts Sheraton Inner Harbor Hotel Baltimore, MD October 17-20, 2010 Chemical Sciences, Geosciences, and Biosciences Division Office of Basic Energy Sciences Office of Science U.S. Department of Energy i Cover art is taken from the public domain and can be found at: http://commons.wikimedia.org/wiki/File:Blue_crab_on_market_in_Piraeus_-_Callinectes_sapidus_Rathbun_20020819- 317.jpg This document was produced under contract number DE-AC05-060R23100 between the U.S. Department of Energy and Oak Ridge Associated Universities. The research grants and contracts described in this document are, unless specifically labeled otherwise, supported by the U.S. DOE Office of Science, Office of Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division. ii Foreword This volume provides a record of the 2nd biennial meeting of the Principal Investigators (PIs) funded by the Physical Biosciences program, and is sponsored by the Chemical Sciences, Geosciences, and Biosciences Division of the Office of Basic Energy Sciences (BES) in the U.S. Department of Energy (DOE). Within DOE-BES there are two programs that fund basic research in energy-relevant biological sciences, Physical Biosciences and Photosynthetic Systems. These two Biosciences programs, along with a strong program in Solar Photochemistry, comprise the current Photo- and Bio- Chemistry Team. This meeting specifically brings together under one roof all of the PIs funded by the Physical Biosciences program, along with Program Managers and staff not only from DOE-BES, but also other offices within DOE, the national labs, and even other federal funding agencies. Of course we also have some distinguished speakers who we hope will stimulate your thinking, and inform you about new tools and resources that will allow you to meet - or exceed - your current research objectives; more on that below. Our objective in holding these research meetings is to provide an environment that (1) encourages free exchange of information on your DOE-funded work; (2) facilitates new collaborations between individual research groups with complementary strengths; (3) allows opportunities for discussions with DOE Program Managers and staff; (4) exposes you to new ideas and methodologies; and (5) supplies information on DOE User Facilities, and how one goes about gaining access to them. In that regard, this year’s agenda features several invited speakers from the DOE national labs. We are delighted to feature Allen Orville from Brookhaven National Laboratory as one of our featured “idea- generators” on the physical science side, and Bryan Linggi and John Cort from the Pacific Northwest National Laboratory (PNNL) who will tell you about the exciting “-omics” capabilities at PNNL’s Environmental Molecular Sciences Lab (EMSL) – and how one goes about accessing them. Ian Carmichael from the Notre Dame Radiation Laboratory has also been invited to provide a brief talk on how he and his colleagues are trying to address the serious problem of radiation damage to protein structures that is caused by x-ray beam lines, and why it is a critically important problem to address. While we extend a warm welcome and our sincere appreciation to our invited speakers, the real star at this year’s meeting is…you. It is your hard work, creativity, productivity, and commitment to world- class science that comes across in your submitted abstracts. Whether you are delivering a talk or presenting a poster, we are sincerely appreciative of your contribution to this meeting. The depth and breadth of the DOE-BES Biosciences portfolio is what makes a meeting like this not only exciting, but also – we hope – a very fun and rewarding one to attend. It has been an extraordinary period of time in DOE’s Office of Science, and we want to thank you for your many contributions to the successful execution of the many calls we have put out over the last two years. Finally, we also wish to thank Diane Marceau from DOE-BES and Connie Lansdon from Oak Ridge Institute for Science and Education (ORISE) for their invaluable help in planning and successfully executing the many logistical tasks associated with putting on this meeting. Robert J. Stack, Program Manager, Physical Biosciences, DOE-BES B. Gail McLean, Program Manager, Photosynthetic Systems, DOE-BES Richard V. Greene, Lead, Photo- and Bio-Chemistry Team, DOE-BES iii iv Agenda Agenda AGENDA 2010 Physical Biosciences Research Meeting Sheraton Inner Harbor Hotel, Baltimore, MD October 17-20, 2010 Sunday, October 17, 2010 3:00 – 6:00 p.m. Registration 5:30 – 6:30 Reception (No Host) 6:30 – 7:30 Dinner at Sheraton Inner Harbor Hotel 7:30 – 8:00 Welcome, Opening Remarks, and DOE Update/News Robert Stack, Program Manager, Physical Biosciences, DOE-BES Eric Rohlfing, Director, Chemical Sciences, Geosciences & Biosciences Division, DOE-BES Monday, October 18, 2010 7:15 – 8:00 a.m. Continental Breakfast Session I: Physical Science Tools for Energy Transduction Studies 8:00 – 8:30 a.m. Welcome and Physical Biosciences Program Update Robert Stack, Program Manager, Physical Biosciences 8:30 – 9:30 More than Simply Atomic Structure: Correlated Single-Crystal Spectroscopy and X-ray Diffraction Allen Orville, Brookhaven National Laboratory 9:30 – 10:00 Break Session II: Hydrogen Metabolism and Electron Flux in Microbial Systems Joe Krzycki, Moderator 10:00 – 10:30 Enzymology of Methanogenesis: Mechanism of Methyl-Coenzyme M Reductase Stephen Ragsdale, University of Michigan 10:30 – 11:00 Electron Bifurcation and Novel Pathways of Electron Flow from Formate in a Model Hydrogenotrophic Methanogen John Leigh, University of Washington 11:00 – 11:30 Genetics and Molecular Biology of Hydrogen Metabolism in Sulfate- Reducing Bacteria Judy Wall, University of Missouri 11:30 – 12:00 Genetic Analysis of Hydrogenotrophic Methanogenesis in Methanosarcina Species William Metcalf, University of Illinois 12:00 – 1:00 Lunch Session III: Plant Growth and Regulation Gloria Coruzzi, Moderator 1:00 – 1:30 Regulation of Actin Filament Ends: The Role of Capping Protein in Stochastic Dynamics and Organelle Behavior Christopher Staiger, Purdue University v 1:30 – 2:00 Cellulose Synthesis and the Control of Growth Anisotropy Tobias Baskin, University of Massachusetts 2:00 – 2:30 Exploring Molecular Mechanisms of Lignin Biosynthesis and Its Regulation Chang-Jun Liu, Brookhaven National Laboratory Session IV: Special Guest Lecture/Life Sciences Research Fellow Bob Stack, Moderator 2:30 – 3:00 Spatial and Temporal Organization of Cyanobacterial Metabolism David Savage, Harvard Medical School 3:00 – 6:00 Free/Discussion Time (Put up your poster too!) 6:00 – 6:30 Reception (No-Host) 6:30 – 7:30 Dinner at Sheraton Inner Harbor Hotel Poster Session I 7:30 – 9:30 Odd Numbered Posters (No-Host) Tuesday, October 19, 2010 7:15 – 8:00 a.m. Continental Breakfast Session V: ‘Omics Tools for Energy Transduction Studies Bob Stack, Moderator 8:00 – 9:00 EMSL: A National Scientific User Facility for State-of-the-Art Molecular and Environmental Research Bryan Linggi & John Cort, EMSL, Pacific Northwest National Laboratory 9:00 – 9:30 Break Session VI: Signal Transduction in Plants Elizabeth Vierling, Moderator 9:30 – 10:00 A Proteomic Study of Brassinosteroid Responses in Plants Zhiyong Wang, Carnegie Institute 10:00 – 10:30 The Role of Auxin in Ambient Temperature Growth Regulation Mark Estelle, University of California, San Diego 10:30 – 11:00 Plant Response to LCO/CO Signals Gary Stacey, University of Missouri 11:00 – 11:30 The Crystal Structure of a Self-Activating Gα Protein Reveals a New Mechanism of Signal Initiation Alan Jones, University of North Carolina Session VII: The Archaeal Proteasome Rick Vierstra, Moderator 11:30 – 12:00 Proteasomes and Post-translational Modification of Haloferax volcanii Proteins Julie Maupin-Furlow, University of Florida 12:00 – 1:00 Lunch vi Session VIII: Pumps, Transporters, and Trafficking in Plants Julian Schroeder, Moderator 1:00 – 1:30 Molecular Mechanism and Biological Function of the Plasma Membrane Proton Pump (H+-ATPase) of Arabidopsis thaliana Michael Sussman, University of Wisconsin Biotechnology Center 1:30 – 2:00 FKBP-Mediated Maturation and Sterol Packing of the Arabidopsis ABCB19 Auxin Transporter are Distinct Processes Angus Murphy, Purdue University 2:00 – 2:30 Trafficking to the Plant Storage Vacuoles in Plants Natasha Raikhel, University of California, Riverside 2:30 – 3:00 Functional Analysis of Plant Sucrose Transporters John Ward, University of Minnesota 3:00 – 7:30 Free/Discussion Time and Dinner on Your Own Poster Session II 7:30 – 9:30 Even Numbered Posters (No-Host) Wednesday, October 20, 2010 7:15 – 8:00 a.m. Continental Breakfast Session IX: Meeting the Challenges of X-ray Studies Bob Stack, Moderator 8:00 – 8:30 Radiation Damage in Macromolecular Crystallography Ian Carmichael, Notre Dame Radiation Laboratory 8:30 – 9:00 Energetics and Structure of the ZIP Metal Transporter Dax Fu, Brookhaven National Laboratory 9:00 – 9:30 Break Session X: Bio-inspired Structural Design Jay Groves, Moderator 9:30 – 10:00 Engineering Functional Scaffolds by Supramolecular Self-Assembly David Lynn, Emory University 10:00 – 10:30 Nanotube-Supported Phospholipid Bilayers: Self-Assembly and Nanoscale Confinement Alex Smirnov, North Carolina
Recommended publications
  • Overexpression of RPN2 Suppresses Radiosensitivity of Glioma Cells By
    Li et al. Molecular Medicine (2020) 26:43 Molecular Medicine https://doi.org/10.1186/s10020-020-00171-5 RESEARCH ARTICLE Open Access Overexpression of RPN2 suppresses radiosensitivity of glioma cells by activating STAT3 signal transduction Changyu Li1†, Haonan Ran2†, Shaojun Song1, Weisong Liu3, Wenhui Zou1, Bei Jiang4, Hongmei Zhao5 and Bin Shao6* Abstract Background: Radiation therapy is the primary method of treatment for glioblastoma (GBM). Therefore, the suppression of radioresistance in GBM cells is of enormous significance. Ribophorin II (RPN2), a protein component of an N-oligosaccharyl transferase complex, has been associated with chemotherapy drug resistance in multiple cancers, including GBM. However, it remains unclear whether this also plays a role in radiation therapy resistance in GBM. Methods: We conducted a bioinformatic analysis of RPN2 expression using the UCSC Cancer Genomics Browser and GEPIA database and performed an immunohistochemical assessment of RPN2 expression in biopsy specimens from 34 GBM patients who had received radiation-based therapy. We also studied the expression and function of RPN2 in radiation-resistant GBM cells. Results: We found that RPN2 expression was upregulated in GBM tumors and correlated with poor survival. The expression of RPN2 was also higher in GBM patients with tumor recurrence, who were classified to be resistant to radiation therapy. In the radiation-resistant GBM cells, the expression of RPN2 was also higher than in the parental cells. Depletion of RPN2 in resistant cells can sensitize these cells to radiation-induced apoptosis, and overexpression of RPN2 had the reverse effect. Myeloid cell leukemia 1 (MCL1) was found to be the downstream target of RPN2, and contributed to radiation resistance in GBM cells.
    [Show full text]
  • Precursor of Ether Phospholipids Is Synthesized by a Flavoenzyme
    Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis Simone Nencia, Valentina Pianoa, Sara Rosatib, Alessandro Alivertic, Vittorio Pandinic, Marco W. Fraaijed, Albert J. R. Heckb, Dale E. Edmondsone, and Andrea Mattevia,1 aDepartment of Biology and Biotechnology, University of Pavia, 27100 Pavia, Italy; bBiomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University and Netherlands Proteomics Centre, 3584 CH Utrecht, The Netherlands; cDepartment of Biosciences, University of Milan, 20133 Milan, Italy; dMolecular Enzymology Group, University of Groningen, 9747 AG Groningen, The Netherlands; and eDepartment of Biochemistry, Emory University, Atlanta, GA 30322 Edited by Emil F. Pai, Ontario Cancer Institute/Princess Margaret Hospital, Toronto, ON, Canada, and accepted by the Editorial Board October 5, 2012 (received for review August 31, 2012) The precursor of the essential ether phospholipids is synthesized ADPS enzymes, whereas type 1 arises from mutations in PEX7, by a peroxisomal enzyme that uses a flavin cofactor to catalyze the protein mediating the peroxisomal import of ADPS (9–12). a reaction that does not alter the redox state of the substrates. Here we report a structural and mechanistic investigation of The enzyme crystal structure reveals a V-shaped active site with mammalian ADPS in WT and mutated forms. The biochemical a narrow constriction in front of the prosthetic group. Mutations hallmark of the enzyme is that it uses a redox cofactor, flavin causing inborn ether phospholipid deficiency, a very severe adenine dinucleotide (FAD), to catalyze a reaction that does not genetic disease, target residues that are part of the catalytic alter the redox state of the substrates (10, 13).
    [Show full text]
  • Prognostic Significance of Autophagy-Relevant Gene Markers in Colorectal Cancer
    ORIGINAL RESEARCH published: 15 April 2021 doi: 10.3389/fonc.2021.566539 Prognostic Significance of Autophagy-Relevant Gene Markers in Colorectal Cancer Qinglian He 1, Ziqi Li 1, Jinbao Yin 1, Yuling Li 2, Yuting Yin 1, Xue Lei 1 and Wei Zhu 1* 1 Department of Pathology, Guangdong Medical University, Dongguan, China, 2 Department of Pathology, Dongguan People’s Hospital, Southern Medical University, Dongguan, China Background: Colorectal cancer (CRC) is a common malignant solid tumor with an extremely low survival rate after relapse. Previous investigations have shown that autophagy possesses a crucial function in tumors. However, there is no consensus on the value of autophagy-associated genes in predicting the prognosis of CRC patients. Edited by: This work screens autophagy-related markers and signaling pathways that may Fenglin Liu, Fudan University, China participate in the development of CRC, and establishes a prognostic model of CRC Reviewed by: based on autophagy-associated genes. Brian M. Olson, Emory University, United States Methods: Gene transcripts from the TCGA database and autophagy-associated gene Zhengzhi Zou, data from the GeneCards database were used to obtain expression levels of autophagy- South China Normal University, China associated genes, followed by Wilcox tests to screen for autophagy-related differentially Faqing Tian, Longgang District People's expressed genes. Then, 11 key autophagy-associated genes were identified through Hospital of Shenzhen, China univariate and multivariate Cox proportional hazard regression analysis and used to Yibing Chen, Zhengzhou University, China establish prognostic models. Additionally, immunohistochemical and CRC cell line data Jian Tu, were used to evaluate the results of our three autophagy-associated genes EPHB2, University of South China, China NOL3, and SNAI1 in TCGA.
    [Show full text]
  • Aneuploidy: Using Genetic Instability to Preserve a Haploid Genome?
    Health Science Campus FINAL APPROVAL OF DISSERTATION Doctor of Philosophy in Biomedical Science (Cancer Biology) Aneuploidy: Using genetic instability to preserve a haploid genome? Submitted by: Ramona Ramdath In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Science Examination Committee Signature/Date Major Advisor: David Allison, M.D., Ph.D. Academic James Trempe, Ph.D. Advisory Committee: David Giovanucci, Ph.D. Randall Ruch, Ph.D. Ronald Mellgren, Ph.D. Senior Associate Dean College of Graduate Studies Michael S. Bisesi, Ph.D. Date of Defense: April 10, 2009 Aneuploidy: Using genetic instability to preserve a haploid genome? Ramona Ramdath University of Toledo, Health Science Campus 2009 Dedication I dedicate this dissertation to my grandfather who died of lung cancer two years ago, but who always instilled in us the value and importance of education. And to my mom and sister, both of whom have been pillars of support and stimulating conversations. To my sister, Rehanna, especially- I hope this inspires you to achieve all that you want to in life, academically and otherwise. ii Acknowledgements As we go through these academic journeys, there are so many along the way that make an impact not only on our work, but on our lives as well, and I would like to say a heartfelt thank you to all of those people: My Committee members- Dr. James Trempe, Dr. David Giovanucchi, Dr. Ronald Mellgren and Dr. Randall Ruch for their guidance, suggestions, support and confidence in me. My major advisor- Dr. David Allison, for his constructive criticism and positive reinforcement.
    [Show full text]
  • Differential Expression of RPN2 in Human Epithelial Ovarian
    Differential expression of ribophorin II in human epithelial ovarian cancer. Shahan Mamoor, MS1 [email protected] East Islip, NY USA Epithelial ovarian cancer (EOC) is the most lethal gynecologic cancer (1). We performed discovery of genes associated with epithelial ovarian cancer and of the high-grade serous ovarian cancer (HGSC) subtype, using published microarray data (2, 3) to compare global gene expression profiles of normal ovary or fallopian tube with that of primary tumors from women diagnosed with epithelial ovarian cancer or HGSC. We identified the gene encoding ribophorin II, RPN2, as among the genes whose expression was most different in epithelial ovarian cancer as compared to the normal fallopian tube. RPN2 expression was significantly higher in high-grade serous ovarian tumors relative to normal fallopian tube. These data indicate that expression of RPN2 is perturbed in epithelial ovarian cancers broadly and in ovarian cancers of the HGSC subtype. RPN2 may be relevant to pathways underlying ovarian cancer initiation (transformation) or progression. Keywords: ovarian cancer, epithelial ovarian cancer, HGSC, high-grade serous ovarian cancer, systems biology of ovarian cancer, targeted therapeutics in ovarian cancer. 1 The five-year survival rate for women diagnosed with high-grade serous ovarian cancer is between 30-40% and has not changed significantly in decades (4, 5). The development of novel, targeted therapeutics to treat HGSC can be facilitated by an enhanced understanding of the transcriptional behavior of ovarian tumors relative to that of the normal ovary. We mined published microarray data (2, 3) to compare global gene expression profiles between human ovarian tumors, including that of the HGSC subtype, and that of normal ovarian and fallopian tissue.
    [Show full text]
  • Identification of Potential Pathogenic Genes Associated with Osteoporosis
    610.BJBJR0010.1302/2046-3758.612.BJR-2017-0102 research-article2017 Freely available online OPEN ACCESS BJR RESEARCH Identification of potential pathogenic genes associated with osteoporosis Objectives B. Xia, Osteoporosis is a chronic disease. The aim of this study was to identify key genes in osteo- Y. Li, porosis. J. Zhou, Methods B. Tian, Microarray data sets GSE56815 and GSE56814, comprising 67 osteoporosis blood samples L. Feng and 62 control blood samples, were obtained from the Gene Expression Omnibus database. Differentially expressed genes (DEGs) were identified in osteoporosis using Limma pack- Jining No. 1 People’s age (3.2.1) and Meta-MA packages. Gene Ontology and Kyoto Encyclopedia of Genes and Hospital, Jining, Genomes enrichment analyses were performed to identify biological functions. Further- Shandong Province, more, the transcriptional regulatory network was established between the top 20 DEGs and China transcriptional factors using the UCSC ENCODE Genome Browser. Receiver operating char- acteristic (ROC) analysis was applied to investigate the diagnostic value of several DEGs. Results A total of 1320 DEGs were obtained, of which 855 were up-regulated and 465 were down- regulated. These differentially expressed genes were enriched in Gene Ontology terms and Kyoto Encyclopedia of Genes and Genomes pathways, mainly associated with gene expres- sion and osteoclast differentiation. In the transcriptional regulatory network, there were 6038 interactions pairs involving 88 transcriptional factors. In addition, the quantitative reverse transcriptase-polymerase chain reaction result validated the expression of several genes (VPS35, FCGR2A, TBCA, HIRA, TYROBP, and JUND). Finally, ROC analyses showed that VPS35, HIRA, PHF20 and NFKB2 had a significant diagnostic value for osteoporosis.
    [Show full text]
  • Highly Thermostable and Alkaline Α-Amylase from a Halotolerant- Alkaliphilic Bacillus Sp. Ab68
    Brazilian Journal of Microbiology (2008) 39:547-553 ISSN 1517-8382 HIGHLY THERMOSTABLE AND ALKALINE α-AMYLASE FROM A HALOTOLERANT- ALKALIPHILIC BACILLUS SP. AB68 Ashabil Aygan1*; Burhan Arikan2; Hatice Korkmaz2; Sadik Dinçer2; Ömer Çolak2 1Kahramanmaras Sutcu Imam University, Faculty of Science and Letters, Department of Biology, K. Maras, Turkey; 2Cukurova University, Faculty of Science and Letters, Department of Biology, Molecular Biology Laboratory, Adana, Turkey Submitted: August 13, 2007; Returned to authors for corrections: October 22, 2007; Approved: July 16, 2008. ABSTRACT An alkaliphilic and highly thermostable α-amylase producing Bacillus sp. was isolated from Van soda lake. Enzyme synthesis occurred at temperatures between 25ºC and 40ºC. Analysis of the enzyme by SDS-PAGE revealed a single band which was estimated to be 66 kDa. The enzyme was active in a broad temperature range, between 20ºC and 90ºC, with an optimum at 50ºC; and maximum activity was at pH 10.5. The enzyme was almost completely stable up to 80ºC with a remaining activity over 90% after 30 min pre-incubation. Thermostability was not increased in the presence of Ca2+. An average of 75% and 60ºC of remaining activity was observed when the enzyme was incubated between pH 5 and 9 for 1 h and for 2 h, respectively. The activity of the enzyme was inhibited by SDS and EDTA by 38% and 34%, respectively. Key words: Bacillus sp., α-amylase, Alkaliphilic, Thermostable, Enzyme. INTRODUCTION unique, buffered haloalkaline habitat appropriate for a stable development of obligately (halo)alkaliphilic microorganisms Amylases are one of the most important industrial enzymes. growing optimally at pH around 10 (39).
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 9,689,046 B2 Mayall Et Al
    USOO9689046B2 (12) United States Patent (10) Patent No.: US 9,689,046 B2 Mayall et al. (45) Date of Patent: Jun. 27, 2017 (54) SYSTEM AND METHODS FOR THE FOREIGN PATENT DOCUMENTS DETECTION OF MULTIPLE CHEMICAL WO O125472 A1 4/2001 COMPOUNDS WO O169245 A2 9, 2001 (71) Applicants: Robert Matthew Mayall, Calgary (CA); Emily Candice Hicks, Calgary OTHER PUBLICATIONS (CA); Margaret Mary-Flora Bebeselea, A. et al., “Electrochemical Degradation and Determina Renaud-Young, Calgary (CA); David tion of 4-Nitrophenol Using Multiple Pulsed Amperometry at Christopher Lloyd, Calgary (CA); Lisa Graphite Based Electrodes', Chem. Bull. “Politehnica” Univ. Kara Oberding, Calgary (CA); Iain (Timisoara), vol. 53(67), 1-2, 2008. Fraser Scotney George, Calgary (CA) Ben-Yoav. H. et al., “A whole cell electrochemical biosensor for water genotoxicity bio-detection”. Electrochimica Acta, 2009, 54(25), 6113-6118. (72) Inventors: Robert Matthew Mayall, Calgary Biran, I. et al., “On-line monitoring of gene expression'. Microbi (CA); Emily Candice Hicks, Calgary ology (Reading, England), 1999, 145 (Pt 8), 2129-2133. (CA); Margaret Mary-Flora Da Silva, P.S. et al., “Electrochemical Behavior of Hydroquinone Renaud-Young, Calgary (CA); David and Catechol at a Silsesquioxane-Modified Carbon Paste Elec trode'. J. Braz. Chem. Soc., vol. 24, No. 4, 695-699, 2013. Christopher Lloyd, Calgary (CA); Lisa Enache, T. A. & Oliveira-Brett, A. M., "Phenol and Para-Substituted Kara Oberding, Calgary (CA); Iain Phenols Electrochemical Oxidation Pathways”, Journal of Fraser Scotney George, Calgary (CA) Electroanalytical Chemistry, 2011, 1-35. Etesami, M. et al., “Electrooxidation of hydroquinone on simply prepared Au-Pt bimetallic nanoparticles'. Science China, Chem (73) Assignee: FREDSENSE TECHNOLOGIES istry, vol.
    [Show full text]
  • Studies Into the Structural Basis of the DNA Uridine Endonuclease Activity of Exonuclease III Homolog Mth212
    Studies into the structural basis of the DNA uridine endonuclease activity of exonuclease III homolog Mth212 Dissertation zur Erlangung des Doktorgrades der Mathematisch-Naturwissenschaftlichen Fakultäten der Georg-August Universität zu Göttingen Vorgelegt von Khaliun Tseden aus Greifswald, Deutschland Göttingen 2011 D7 Referent: Prof. Dr. Hans-Joachim Fritz Korreferent: PD Dr. Wilfried Kramer Tag der mündlichen Prüfung: 02. Mai 2011 TABLE OF CONTENTS Table of Contents 1 Introduction ………………………………………………………………….. 1 1.1. Background to the study ………………………………………………… 1 1.1.1. Necessity of mutation avoidance………………………………… 1 1.1.2. Mutations arising in DNA during replication …………………… 1 1.1.3. Exogenous sources of DNA damage …………………………….. 2 1.1.4. Endogenous sources of DNA damage …………………………… 2 1.1.4.1. Hydrolytic DNA deamination ........……………………… 4 1.1.5. Repair of uracil in DNA …………………………………………. 5 1.1.5.1. Uracil-initiated base excision repair …………………...... 5 1.1.5.2. Uracil-initiated nucleotide incision repair ……………… 7 1.2. Objective and methodology of the study ………………………………… 9 1.2.1. Objective of the study.…………………………………………… 9 1.2.2. Methodology of the study ………………………………………. 9 1.2.2.1. Necessity of screening or selection methodology in 11 directed evolution of enzymes …………………………………………… 1.2.2.2. Selection of a protein with acquired DNA uridine 11 endonuclease activity ………………………………………………….... 2. Materials and Methods ………………………………………………………. 13 2.1. Materials …………………………………………………………………. 13 2.1.1. Bacterial strains ………………………………………………….. 13 2.1.1.1. Escherichia coli …………………………………………. 13 2.1.1.2. Bacillus subtilis ………………………………………… 14 2.1.2. Bacteriophage strains …………………………………………….. 14 2.1.3. Plasmid vectors ………………………………………………… 15 2.1.4. 2’ Desoxyriboseoligonucleotides ………………………………. 17 2.1.5. Molecular ladders and markers ………………………………….. 21 2.1.6.
    [Show full text]
  • How Nature Can Exploit Nonspecific Catalytic and Carbohydrate Binding
    How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity Fiona Cuskina,b,1, James E. Flinta,1, Tracey M. Glosterc,1,2, Carl Morlanda, Arnaud Basléa, Bernard Henrissatd, Pedro M. Coutinhod, Andrea Strazzullie, Alexandra S. Solovyovaa, Gideon J. Daviesc, and Harry J. Gilberta,b,3 aInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom; bThe Complex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602; cStructural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom; dArchitecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 7257, 13288 Marseille Cedex 9, France; and eInstitute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, 80131 Naples, Italy Edited by Arnold L. Demain, Drew University, Madison, NJ, and approved October 30, 2012 (received for review July 16, 2012) Noncatalytic carbohydrate binding modules (CBMs) are components CBMs enhance the activity of their cognate enzymes, and though of glycoside hydrolases that attack generally inaccessible substrates. the mechanism(s) by which this occurs remains uncertain, CBMs CBMs mediate a two- to fivefold elevation in the activity of endo- most likely fulfill a targeting function by increasing the effective acting enzymes, likely through increasing the concentration of the concentration of the appended enzymes, in the vicinity of the appended enzymes in the vicinity of the substrate. The function of substrate, thereby enhancing catalytic efficiency (8, 9). CBMs appended to exo-acting glycoside hydrolases is unclear Fructans, such as inulin and levan (polymers of predominantly because their typical endo-binding mode would not fulfill a target- β-2,1– or β-2,6–linked fructose units, respectively) are common ing role.
    [Show full text]
  • Supplementary Data
    SUPPLEMENTARY DATA Table S1. List of 114 proteins identified in RT TEX but not UT-TEXA Cdv3 Adss Actr2 Ptma;Gm6625 Tes;Gm4985 Srm Tceb1 Tpt1 Bri3bp Tardbp Gng2 Tmx3 Eif5a Gnb2l1 Kiaa1467 Epb4.1;Epb41 Tuba4a;Tuba8 Sept11;Sept6 Rbmx;Rbmxl1 Oas1g;Oas1a Rangap1 Rbbp7 Hsd17b12 Pygb Nrd1 Npepps Slco4a1 Bcat1 Scamp3;Tu52 Eif3l Tfg Farsb Eif3c Otub1 Aqp1 Lrrc8c Qdpr Ctsb Ciapin1 Sec11a Khsrp Rab14 Sqstm1 Adcy7 Brk1 Snrpa Hist1h1d;Hist1h1c Vcam1 Eif4g1 Prkcsh Rab31 Cse1l Tm9sf3 Taldo1 Alcam Naca Gps1 Ide Ptgs2 Kars Atp11a Dnajc13 Eif3e Psme1 Rap1a;Gm9392 Tmem33 Spr Kpna4;Kpna3 Tars Cyb5;Cyb5a Kpna2 Apmap Utrn Dbi Gsdmdc1 Pld3 Rpl14 Alad Api5 Dnaja1 Ipo7 Atp2a2;Atp2a1 Irgm1;Ifggd3 Tnfrsf23;Tnfrsf22 Vamp8 Rbbp4 Slc9a3r2 Cpd Cdc37 Hspe1-rs1;Hspe1 Pdia4 Bcap31 Uchl3;Uchl4 Aprt Rpn2 Tcirg1 Gpx1 Mpp1 Sigirr Rps16 Adh5 Txnrd1 Gstp1 Scrib Galk1 F3 Usp14 Asah1 Gna13 Slc9a1;Slc9a2 Gipc1 Psmb8 Nceh1 Rpl13a A A single protein, Rpl10a, was present in UT-TEX but not RT-TEX Table S2. Shared pathways predicted by IPA to be activated or inhibited in RT TEX as compared to UT-TEX ACTIVATED Z-score P-value INHIBITED Z-score P-value Thrombin Signaling 2.236 0.009 STAT3 Pathway -2 0.003954052 Tec Kinase Signaling 2.000 0.004 RhoGDI Signaling -1.667 4.0245E-07 Actin Cytoskeleton Signaling 1.941 1.57285E-08 PPAR Signaling -1 0.009262858 CXCR4 Signaling 1.890 0.000663358 PI3K/AKT Signaling 1.633 0.000815054 Cardiac Hypertrophy Signaling 1.633 0.00491384 Integrin Signaling 1.508 4.06632E-06 Regulation of Actin-based Motility by Rho 1.414 1.42092E-06 Phospholipase C Signaling
    [Show full text]
  • 154581A0.Pdf
    No. 3914, NOVEMBER 4, 1944 NATURE 581 Alleged Role of Fructofuranose in the ture of fructofuranoses and fructopyranoses. The recent demonstration that glucose-1-phosphate (Cori Synthesis of Levan ester) and fructose form a dynamic equilibrium with THE view was long widely entertained that cells sucrose and phosphoric acid in the presence of a. synthesize macromolecules of polysaccharides and specific enzyme8 corroborates this view. Addition of proteins by a reversion .of the process of hydrolysis. fructose to sucrose does not inhibit levan production It has been suggested accordingly that the synthesis from the latter, yet fructose itself, although it pre­ of the polyfructoside levan specifically from aldo­ sumably contains ready fructofuranose, is not con­ side< >fructofuranosides (sucrose, raffinose) involves verted into levan by levansucrase7 • Similarly, levan­ two distinct steps : first, hydrolysis of the substrate ; sucrase fails to form levan from reaction mixtures secondly, polymerization of fructofuranose b;r a con­ in which fructofuranose is sustainedly liberated in densation involving removal of water1• Bacteria statu nascendi, for example, in reaction mixtures of which form levan from sucrose do so also from methyl gamma fructoside + yeast invertase, and of raffinose•. This polymerative type of sucrose de­ inulin inulase. gradation is concurrent with an ordinary hydrolytic (c) Extracts of an Aerobacter, although they pro­ inversions·'· The same banteria ferment !evans. duce levan from sucrose and hydro'yse the latter as Investigators might be tempted by these correlations well, do not hydrolyse levan. Thus they contain to consider the enzyme system, levansucrase, to be levansucrase and invertase but no polyfructosidase but a mixture of invertase and polyfructosidase.
    [Show full text]