NCI Laboratory of Molecular Biology Oral History Project Interview #1 with Dr
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From the President's Desk
Sept | Oct 2009 From the President’s desk: The Increasing Importance of Model Organism Research I’m sure you know this scenario: You’re at a party, and someone hears you’re a biologist, and asks, “What do you work on?” When this happens to me, and I respond that I study yeast, I frequently get the follow-up question that you have probably already anticipated: “Are you learning how to make better beer?” At that point, I offer my explanation about the value of studying model organisms, which in cludes the statement that my daughter, now 17, learned to repeat with me by the time she was 3: “Yeast are actually a lot like people.” If you study a model organism, whether it’s yeast, bacteria, phage, flies, worms, fish, plants, or something else, you probably have been in Fred Winston a similar situation when talking to someone who is not a scientist. There GSA President is little understanding among the general public about the value of studying a model organism. This is also true among some who we might think would better understand this issue. While you wouldn’t be surprised to learn that the person at this party was a lawyer or a businessperson, you might also not be too surprised if that person turned out to be a physician, or even a human biologist. Even among some biologists who understand the history of model organisms, there may be a lack of appreciation for what model organism research can contribute to future scientific understanding. For these scientists, model organi sms appear to be in the twilight of their usefulness with the advent of new sequencing technologies and other genome-wide, high-throughput approaches that can be used in human studies. -
CURRICULUM VITAE Laura Finzi
CURRICULUM VITAE Laura Finzi Physics Department, Emory University e-mail: [email protected] 400 Dowman Dr, Atlanta, GA 30322 http://www.physics.emory.edu/faculty/finzi/ tel. 404-727-4930 ; fax: 404-727-0873 EDUCATION_________________________________________________________________________________ 1990 Ph.D. in Chemistry, University of New Mexico, Albuquerque, NM. (Advisor: Carlos Bustamante) 1987 Master's in Chemistry, University of New Mexico, Albuquerque, NM. 1984 Laurea in Industrial Chemistry, University of Bologna, Bologna, Italy. 1979 Diploma from Liceo Classico "M. Minghetti" (High School diploma), Bologna, Italy. PROFESSIONAL ACTIVITY____________________________________________________________________ September 2012 - present: Full Professor, Physics Department, Emory University. July 2005-August 2012: Associate Professor, Physics Department, Emory University. June 1999-June 2005: Tenured Researcher and Group Leader, Biology Dept, University of Milano, Italy. 1993-May 1999: Researcher (tenured in ’96), Biology Dept, University of Milan, Italy. 1992-1993: Post Doctoral Fellow, Biochemistry Dept., Brandeis University (Mentor: Jeff Gelles). 1990-1991: Post Doctoral Fellow, Chem. Dept., University of New Mexico (October-December 1990), Institute of Molecular Biology, University of Oregon (January-December 1991) (Carlos Bustamante group). HONORS and AWARDS________________________________________________________________________ 2018: Recognized for “Excellent Teaching” by Phi Beta Kappa Mentee. Ceremony held on 4/10 in Cannon Chapel. -
Cold Spring Harbor Symposia on Quantitative Biology
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY VOLUME XLV---PART 1 COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY VOLUME XLV MOVABLE GENETIC ELEMENTS COLD SPRING HARBOR LABORATORY 1981 COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY VOLUME XLV 1981 by The Cold Spring Harbor Laboratory International Standard Book Number 0-87969-044-5 Library of Congress Catalog Card Number 34-8174 Printed in the United States of America All rights reserved COLD SPRING HARBOR SYMPOSIA ON QUANT1TA T1VE BIOLOGY Founded in 1933 by REGINALD G. HARRIS Director of the Biological Laboratory 1924 to 1936 Previous Symposia Volumes I (1933) Surface Phenomena XXIII (1958) Exchange of Genetic Material: Mechanism I1 (1934) Aspects of Growth and Consequences Ili (1935) Photochemical Reactions XX1V (1959) Genetics and Twentieth Century Darwinism IV (1936) Excitation Phenomena XXV (1960) Biological Clocks V (1937) Internal Secretions XXV1 (I 961) Cellular Regulatory Mechanisms VI (1938) Protein Chemistry XXVll (1962) Basic Mechanisms in Animal Virus Biology VII (1939) Biological Oxidations XXVIlI (1963) Synthesis and Structure of Macromolecules VIII (1940) Permeability and the Nature of Cell Mem- XXIX (1964) Human Genetics branes XXX (1965) Sensory Receptors 1X (1941) Genes and Chromosomes: Structure and Organi- XXXI (1966) The Genetic Code zation XXXII (1967) Antibodies X (1942) The Relation of Hormones to Development XXXIlI (1968) Replication of DNA in Microorganisms XI (1946) Heredity and Variation in Microorganisms. XXX1V (1969) The Mechanism of Protein -
Biological Consequences of Tightly Bent DNA: the Other Life of a Macromolecular Celebrity
University of Pennsylvania ScholarlyCommons Department of Physics Papers Department of Physics 10-2006 Biological Consequences of Tightly Bent DNA: The Other Life of a Macromolecular Celebrity Hernan G. Garcia Paul Grayson Lin Han Mandar Inamdar Jané Kondev See next page for additional authors Follow this and additional works at: https://repository.upenn.edu/physics_papers Part of the Physics Commons Recommended Citation Garcia, H. G., Grayson, P., Han, L., Inamdar, M., Kondev, J., Nelson, P. C., Phillips, R., Widom, J., & Wiggins, P. A. (2006). Biological Consequences of Tightly Bent DNA: The Other Life of a Macromolecular Celebrity. Biopolymers, 85 115-130. http://dx.doi.org/10.1002/bip.20627 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/physics_papers/503 For more information, please contact [email protected]. Biological Consequences of Tightly Bent DNA: The Other Life of a Macromolecular Celebrity Abstract The mechanical properties of DNA play a critical role in many biological functions. For example, DNA packing in viruses involves confining the viral genome in a volume (the viral capsid) with dimensions that are comparable to the DNA persistence length. Similarly, eukaryotic DNA is packed in DNA-protein complexes (nucleosomes) in which DNA is tightly bent around protein spools. DNA is also tightly bent by many proteins that regulate transcription, resulting in a variation in gene expression that is amenable to quantitative analysis. In these cases, DNA loops are formed with lengths that are comparable to or smaller than the DNA persistence length. The aim of this review is to describe the physical forces associated with tightly bent DNA in all of these settings and to explore the biological consequences of such bending, as increasingly accessible by single-molecule techniques. -
Ise En Page 1 17/06/10 16:41 Page 1 09
COUV_EXE+TRANCHES_QUADRI+SPE:Mise en page 1 17/06/10 16:41 Page 1 09 ACKNOWLEDGEMENTS HFSPO is grateful for the support of the following organizations: Australia (AU) National Health and Medical Research Council ANNUAL REPORT 20 (NHMRC) Canada (CA) Canadian Institute of Health Research (CIHR) Natural Sciences and Engineering Research Council (NSERC) European Union (EU) 09 European Commission – Directorate General Research (DG RESEARCH) European Commission – Directorate General APRIL 2009 - MARCH 2010 Information Society (DG INFSO) France (FR) Ministère des Affaires Étrangères et Européennes (MAEE) ANNUAL REPORT Ministère de l’Enseignement Supérieur et de la Recherche (MESR) Communauté Urbaine de Strasbourg (CUS) Région Alsace Human Germany (DE) Federal Ministry of Education and Research (BMBF) Frontier India (IN) Science Department of Biotechnology (DBT), Ministry of Science and Technology Program Italy (IT) Ministry of Education, University and Research Japan (JP) Ministry for Economy, Trade and Industry (METI) Ministry of Education, Culture, Sports, Science and Technology (MEXT) Republic of Korea (KR) Ministry of Education, Science and Technology (MEST) New Zealand (NZ) Health Research Council (HRC) Norway (NO) The Research Council of Norway (RCN) Switzerland (CH) State Secretariat for Education and Research (SER) The International Human Frontier Science Program Organization (HFSPO) United Kingdom (UK) 12 quai Saint-Jean - BP 10034 Biotechnology and Biological Sciences Research Council (BBSRC) 67080 Strasbourg CEDEX - France Medical Research Council (MRC) Fax. +33 (0)3 88 32 88 97 e-mail: [email protected] United States of America (US) Website: www.hfsp.org National Institutes of Health (NIH) HUMAN FRONTIER SCIENCE PROGRAM National Science Foundation (NSF) Japanese Website: http://jhfsp.jsf.or.jp HUMAN FRONTIER SCIENCE PROGRAM The Human Frontier Science Program is a unique program funding basic research of the highest quality at the frontier of the life sciences that is 09 innovative, risky and requires international collaboration. -
Genome-Wide Transcriptional Regulation and Chromosome Structural Arrangement by Galr in E
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Frontiers - Publisher Connector ORIGINAL RESEARCH published: 16 November 2016 doi: 10.3389/fmolb.2016.00074 Genome-Wide Transcriptional Regulation and Chromosome Structural Arrangement by GalR in E. coli Zhong Qian 1, Andrei Trostel 1, Dale E. A. Lewis 1, Sang Jun Lee 2, Ximiao He 3, Anne M. Stringer 4, Joseph T. Wade 4, 5, Thomas D. Schneider 6, Tim Durfee 7 and Sankar Adhya 1* 1 Laboratory of Molecular Biology, National Institutes of Health, National Cancer Institute, Bethesda, MD, USA, 2 Microbiomics and Immunity Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Korea, 3 Laboratory of Metabolism, National Institutes of Health, National Cancer Institute, Bethesda, MD, USA, 4 Wadsworth Center, New York State Department of Health, Albany, NY, USA, 5 Department of Biomedical Sciences, School of Public Health, University of Albany, Albany, NY, USA, 6 Gene Regulation and Chromosome Biology Laboratory, National Institutes of Health, National Cancer Institute, Center for Cancer Research, Frederick, MD, USA, 7 DNASTAR, Inc., Madison, WI, USA The regulatory protein, GalR, is known for controlling transcription of genes related to Edited by: D-galactose metabolism in Escherichia coli. Here, using a combination of experimental Tatiana Venkova, University of Texas Medical Branch, and bioinformatic approaches, we identify novel GalR binding sites upstream of several USA genes whose function is not directly related to D-galactose metabolism. Moreover, we do Reviewed by: not observe regulation of these genes by GalR under standard growth conditions. Thus, Maria A. Miteva, Paris Diderot University, France our data indicate a broader regulatory role for GalR, and suggest that regulation by GalR Lucia B. -
DNA Loop.Ing in Cellular Repression of Transcription of the Galactose Operon
Downloaded from genesdev.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press DNA loop.ing in cellular repression of transcription of the galactose operon Nitai Mandal, 1 Wen Su, 2 Roberta Haber, 1 Sankar Adhya, 1 and Harrison Echols 2 1Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892 USA; 2Department of Molecular and Cell Biology, University of California, Berkeley, California 94307 USA Communication between distant DNA sites is a central feature of many DNA transactions. Negative regulation of the galactose (ga/) operon of Escherichia coli requires repressor binding to two operator sites located on opposite sides of the promoter. The proposed mechanism for regulation involves binding of the repressor to both operator sites, followed by a protein-protein association that loops the intervening promoter DNA (double occupancy plus association). To assess these requirements in vivo, we have previously converted ga/operator sites to lac and shown that both operator sites must be occupied by the homologous repressor protein (Lac or Gal) for negative regulation of the ga/operon. We have now addressed more directly the need for protein- protein association by the use of the converted operator sites and a mutant Lac repressor defective in association of the DNA-binding dimers. We have compared the biological and biochemical activity of two Lac repressors: the wild-type (tetramer) I + form, in which the DNA-binding dimer units are tightly associated; and the mutant I "~ repressor, in which the dimer units do not associate effectively. The I ÷ repressor is an efficient negative regulator of the ga/operon in vivo, but the I"~ mutant is an ineffective repressor. -
Characterization of the Integration Protein of Bacteriophage X As a Site
Proc. Nati. Acad. Sci. USA Vol. 74, No. 4, pp. 1511-1515, April 1977 Biochemistry Characterization of the integration protein of bacteriophage X as a site-specific DNA-binding protein (bacteriophage X int gene/viral integration/site-specific genetic recombination) MICHAEL KOTEWICZ, STEPHEN CHUNG, YOSHINORI TAKEDA, AND HARRISON ECHOLS Department of Molecular Biology, University of California, Berkeley, California 94720 Communicated by H. Fraenkel-Conrat, January 31, 1977 (7), lntC226 (21), intts2001 and intts2004 (38), intam29 (9, ABSTRACT The Int protein specified by bacteriophage X is required for the recombination event that integrates the viral 22), xisl and xls6 (9), Sam7 (23). The phage deletion and/or DNA into the host genome at its specific attachment site. Using substitution mutations used were: b538, deleting the phage a DNA-binding assay, we have partially purified the Int protein attachment site (24); b522, deleting the int and xis genes but and studied some of the features of its binding specificity and not the phage recombination genes (24); gal8, carrying the regulation. The DNA-binding activity is attributed to Int protein bacterial gal operon and the left prophage attachment site ba' because the activity is eliminated by a nonsense mutation or a (25); blo7-20, carrying the bacterial blo operon and the right deletion in the int gene, and is rendered thermolabile by tem- perature-sensitive mutations in the int gene. The DNA-binding prophage attachment site ab' (26); gal8bio7-20, carrying both activity is specific for DNA carrying an appropriate attachment the gal and bNo genes and the bacterial attachment site bb' (1, site, suggesting that Int protein directs the sequence-specific 2, 10 and Fig. -
Adhya Sankar Oral History 2008 B
NCI Laboratory of Molecular Biology Oral History Project Interview #2 with Dr. Sankar L. Adhya Conducted on October 8, 2008, by Jason Gart JG: My name is Jason Gart and I am a senior historian at History Associates Incorporated in Rockville, Maryland. Today’s date is October 8, 2008 and we are in the offices of the National Institutes of Health in Bethesda, Maryland. Please state your full name and also spell it. SA: Sankar Adhya. S-A-N-K-A-R—A-D-H-Y-A. JG: Today I would like to first walk through some questions that came up from the last session. Then we will switch from a chronological to a thematic approach and talk about the role of publications in science, the practice of science, and what has changed. SA: Okay. JG: When we last spoke we were talking about your election to the National Academy of Sciences in 1994. I had a question about the twentieth anniversary reunion. I had the opportunity to watch the videotape of the evening and saw that you gave Dr. Pastan a dinner bell. What was the significance of that gift? SA: Ah, yes. Interview #2 with Dr. Sankar L. Adhya, October 8, 2008 2 JG: Can you explain the significance? SA: I think what happened was that we had a weekly seminar on data club and journal club. At that time there was only one group, everybody participated, both the eukaryotic people and prokaryotic people participated in the same seminar. Later Dr. Pastan divided the groups into two. One was called the vegetables; the bacteria people. -
Phage Summits
Blackwell Science, LtdOxford, UKMMIMolecular Microbiology0950-382XBlackwell Publishing Ltd, 2004? 200455513001314Meeting ReportThe 2004 Phage SummitS. Adhya et al. Molecular Microbiology (2005) 55(5), 1300–1314 doi:10.1111/j.1365-2958.2005.04509.x MicroMeeting 2004 ASM Conference on the New Phage Biology: the ‘Phage Summit’ Sankar Adhya,1 Lindsay Black,2 David Friedman,3 model systems of unequalled power and facility for Graham Hatfull,4 Kenneth Kreuzer,5 Carl Merril,6 studying fundamental biological issues. In addition, Amos Oppenheim,7 Forest Rohwer8 and Ry Young9* the New Phage Biology is also populated by basic and 1Laboratory of Molecular Biology, Center for Cancer applied scientists focused on ecology, evolution, Research, National Cancer Institute, 37 Convent Dr., Rm nanotechnology, bacterial pathogenesis and phage- 5138, Bethesda, MD 20892-4264, USA. based immunologics, therapeutics and diagnostics, 2Department of Biochemistry and Molecular Biology, resulting in a heightened interest in bacteriophages University of Maryland Medical School, 108 N. Greene per se, rather than as a model system. Besides con- Street, Baltimore, MD 21201-1503, USA. stituting another landmark in the long history of a 3Department of Microbiology and Immunology, University field begun by d’Herelle and Twort during the early of Michigan, 5641 Medical Science Building II, Ann Arbor, 20th century, the Summit provided a unique venue for MI 48109-0620, USA. establishment of new interactive networks for collab- 4Pittsburgh Bacteriophage Institute, 4249 5th Avenue, orative efforts between scientists of many different University of Pittsburgh, Pittsburgh, PA 15260, USA. backgrounds, interests and expertise. 5Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710, USA.