JOURNAL of VIROLOGY VOLUME 48 NUMBER 3 DECEMBER 1983 Edward M

Total Page:16

File Type:pdf, Size:1020Kb

JOURNAL of VIROLOGY VOLUME 48 NUMBER 3 DECEMBER 1983 Edward M JOURNAL OF VIROLOGY VOLUME 48 NUMBER 3 DECEMBER 1983 Edward M. Scolnick, Editor in Chief (1987) Merck Sharp & Dolime Research Laboraitories Wes.t Point, Pa. David T. Denhardt, Editor (1987) Robert M. Krug, Editor (1987) University of Western Ontario Sloan-Kettering Institute London, Ontario, Canada New York, N.Y. Bernard N. Fields, Editor (1988) Michael B. A. Oldstone, Editor (1988) Harvard University, Medical School Sc ripps Clinic & Research Fouindation Boston, Mass. La Jolla, Calif. Harold S. Ginsberg, Editor (1984) Robert A. Weisberg, Editor (1988) Coluimbia University National Institlute of Child Health and Human Development New York, N.Y. Bethesda, Md. EDITORIAL BOARD David Baltimore (1984) Alice S. Huang (1984) Harriet Robinson (1985) Amiya K. Banerjee (1985) Tony Hunter (1983) William S. Robinson (1983) Andrew Becker (1985) Masayori Inouye (1985) Bernard Roizman (1985) Tamar Ben-Porat (1984) Robert Kamen (1985) Roland R. Rueckert (1985) Kenneth I. Berns (1985) Thomas J. Kelly, Jr. (1985) Norman P. Salzman (1984) David Botstein (1985) George Khoury (1984) Joseph Sambrook (1985) Dennis T. Brown (1984) Elliott Kieff (1984) Priscilla A. Schaffer (1984) Ahmad I. Bukhari (1984) Jonathan A. King (1984) Sondra Schlesinger (1983) Barrie J. Carter (1984) Daniel Kolakofsky (1983) June R. Scott (1983) Purnell Choppin (1983) Robert Lamb (1985) Bart Sefton (1985) John M. Coffin (1983) Robert A. Lazzarini (1984) Phillip A. Sharp (1985) Geoffrey M. Cooper (1984) Myron Levine (1985) Thomas E. Shenk (1984) Walter Doerfler (1983) Douglas R. Lowy (1983) Charles J. Sherr (1984) Harrison Echols (1984) Robert Martin (1984) Saul J. Silverstein (1985) Elvera Ehrenfeld (1983) George Miller (1984) Lee D. Simon (1984) Robert N. Eisenman (1985) Lois K. Miller (1985) Ann Skalka (1985) Suzanne U. Emerson (1983) Robert C. Miller (1983) Patricia G. Spear (1984) S. Jane Flint (1984) Peter Model (1983) Mark F. Stinski (1983) Yasuhiro Furuichi (1985) Bernard Moss (1983) F. William Studier (1984) Costa Georgopolous (1983) Nancy G. Nossal (1984) Lawrence S. Sturman (1985) Larry M. Gold (1985) J. Thomas Parsons (1983) Jesse Summers (1985) Peter Gruss (1985) Ulf G. Petterson (1983) William Summers (1985) Hidesaburo Hanafusa (1983) Lennart Philipson (1984) John M. Taylor (1984) William S. Hayward (1984) Lewis I. Pizer (1984) Howard M. Temin (1985) John J. Holland (1984) Craig R. Pringle (1983) George F. Vande Woude (1983) Ian H. Holmes (1983) Fred Rapp (1984) Edward K. Wagner (1983) Robert W. Honess (1983) Dan S. Ray (1983) Eckard Wimmer (1985) Nancy Hopkins (1983) M. E. Reichmann (1985) Charles Hamish Young (1983) Peter M. Howley (1984) Gordon M. Ringold (1984) Helen R. Whiteley, Chairman, Publications Boacrd Walter G. Peter III, Direc tor, Publications Linda M. Illig, Managing Editor, Jouirnals Paula R. Ellison, Production Editor The Journal of Virology (ISSN 0022-538X), a publication of the American Society for Microbiology, 1913 1 St., NW. Washington, DC 20006, is devoted to the dissemination of fundamental knowledge concerning viruses of bacteria, plants, and animals. Investigators are invited to submit reports of original research in all areas of basic virology, including biochemistry. biophysics, genetics, immunology, morphology, physiology, and pathogenesis and immunity. Instructions to authors are published in the January issue each year; reprints are available from the editors and the Publications Office. The Jollrnlal is issued monthly, four volumes per year. The nonmember subscription price is $225 per year; single copies are $20. The member subscription price is $37 (foreign, $44 [surface ratel) per year; single copies are $7.00. Correspondence relating to subscriptions, reprints, defective copies, availability of back issues, lost or late proofs. disposition of submitted manuscripts, and general editorial matters should be directed to the ASM Publications Office, 1913 I St., NW, Washington, DC 20006 (area 202 833-9680). Claims for missing issues from residents of the United States, Canada, and Mexico must be submitted within 3 months after publication of the issues; residents of all other countries must submit claims within 6 months of publication of the issues. Claims for issues missing because of failure to report an address change or for issues 'missing from files" will not be allowed. Second-class postage paid at Washington, DC 20006, and at additional mailing offices. POSTMASTER: Send address changes to Jouirnal of Virology, ASM, 1913 I St., NW, Washington. DC 20006. Made in the U.S.A. Copyright © 1983, American Society for Microbiology. (*fdli(f4P(JtkJ. L1'.JI' ( I'1I.t All Rights Reserved. The code at the top of the first page of an article in this journal indicates the copyright owner's consent that copies of the article may be made for personal use or for personal use of specific clients. This consent is given on the condition. however, that the copier pay the stated per-copy fee through the Copyright Clearance Center. 21 Congress St., Salem. MA 01970. for copying beyond that permitted by Sections 107 and 108 of the U.S. Copyright Law. This consent does not extend to other kinds of copying, such as copying for general distribution, for advertising or promotional purposes, for creating new collective works, or for resale. Author Index Aasted, Bent, 573 Hamagishi, Yasutaro, 709 Ricci, William, 667 Andersen, Klaus B., 765 Hanafusa, Hidesaburo, 744 Ronda, Concepci6n, 721 Appella, Ettore, 709 Henry, Berch, II, 580 Roussel, Martine F., 770 Hood, Rachel, 580 Roy, Polly, 627 Hudewentz, J., 731 Ruddle, Frank H., 770 Banks, L., 591 Hughes, Stephen H., 667 Baric, Ralph S., 633 Hunter, Tony, 752 Barker, Peter E., 770 Bishop, J. Michael, 565 Ito, Yoshiaki, 709 Sadowski, Paul D., 647 Bloom, Marshall E., 573 Schlesinger, Sondra, 676 Boone, Lawrence R., 779 Schwarz, E., 731 Bornkamm, G. W., 731 Jolicoeur, Paul, 685 Scolnick, Edward M., 752 Brackmann, Karl H., 604 Segawa, Kaoru, 709 Brewer, Gregory J., 774 Sherr, Charles J., 770 Buekens, Pierre, 697 Kahlon, Jasbir, 627 Sironi, Gianpiero, 616 Klempnauer, Karl-Heinz, 565 Smith, Julie K., 654 Koh, Chong-kun, 779 Sorge, Joe, 667 Cogniaux-LeClerc, Jacqueline, 697 Koprowski, Hilary, 660 Sprecher-Goldberger, Suzanne, Cohen, G., 591 Kramer, Tammo A., 604 697 Cooper, Jonathan A., 752 Stohlman, Stephen A., 633 Costa, R. H., 591 Sugiyama, Kazuo, 627 Cywinski, Anita, 654 Lai, Michael M. C., 633 Symington, Janey S., 604 Laux, G., 731 Lee, Donald, 647 Dalianis, Tina, 709 Levis, Robin, 676 Taylor, John M., 654 DesGroseillers, Luc, 685 L6pez, Rubens, 721 Tennant, Raymond W., 779 Draper, K. G., 591 Lucher, Lynne A., 604 Thiry, Lise, 697 Eisenberg, R., 591 Mayer, Leonard W., 573 Wagner, E. K., 591 Weaver, Robert F., 641 Weiss, Barbara, 676 Foster, David A., 744 Olislager, Roland, 697 Wiktor, Tadeusz J., 660 Freese, U. K., 731 Ou, Chin-yih, 779 Willingham, Mark, 709 Fuchs, L. Yolanda, 641 Ozanne, Brad, 752 Woods, Michael S., 641 Wunner, William H., 660 Garcia, Ernesto, 721 Pagano, Joseph S., 580 Garon, Claude F., 573 Powell, K. L., 591 Yang, Czau-Siung, 580 Ghisotti, Daniela, 616 Yang, Wen K., 779 G6mez, Antonio, 721 Goto, Ronald M., 774 Raab-Traub, Nancy, 580 Green, Maurice, 604 Reagan, Kevin J., 660 Zangrossi, Sandro, 616 ACKNOWLEDGMENT The following have served as invited special reviewers for the Journal during 1983, and their help is greatly appreciated. Stu Aaronson Diane Cuppels Berg Hampar Sankar Adhya Samuel Dales Daniel Hardy Rafi Ahmed Vittorio Defendi Janet Hartley Charles A. Alford, Jr. Mel DePamphilis William Haseltine James Alwine Ravi Dhar John Hassell Robert Anderson Jules L. Dienstag Stanley Hattman Steven Anderson Dan Dimaio Anne M. Haywood Ralph Arlinghaus George Dimayorca Ari Helenius Richard Armentrout Dino Dina Roger Hendrix Richard Axel Martin E. Dorf Roger Hewitt Howard L. Bachrach R. Gordon Douglas Lawrence Hightower John Bader Walter Dowdle Maurice R. Hilleman George Baer Gordon Dreesman Shalom Z. Hirschman Corrado Baglioni Gideon Dreyfus Monto Ho L. Andrew Ball Peter Duesberg John J. Holland Marcel Baluda Walter Eckhart F. Blaine Hollinger Mariano Barbacid John Elder John A. Holowczak J. Richard Baringer Ron Ellis Marshall Horwitz Samuel Baron Francis A. Ennis Sally Huber Renato Baserga Lynne Enquist Joe Hughes Claudio Basilico Marcia J. Ensinger Jerry Hurwitz Robert Bassin Lois B. Epstein Richard Hyman Karen Beeman H. Gunti Erdl James N. Ihle Thomas Benjamin Raymond Erikson Mark Israel Arnold Berk Max Essex Yoshiaki Ito Anna Bialkowska Mary Kolb Estes Gilbert Jay David Bishop Anthony S. Fauci Richard T. Johnson Michael Bishop Gerald Fink Wolfgang Joklik Klaus Bister James B. Flanegan David Kabat Donald Blair Erwin Fleissner Albert Kapikian Barry Bloom Stephen C. Foster Robert S. Kauffman Marshall E. Bloom Michael M. Frank Vicki E. Kelley David Boettinger Robert Friedman D. C. Kelly Dani Bolognesi Ted Friedman Eli Keshet Michael Botchan Mark Furth Edwin D. Kilbourne Pierre Bourgaux Robert Gallo Saul Kit Joan Brugge Anthony Garro David Knipe Michael Buchmeier E. Peter Geidushek Christine Kozak Steven Burakoff Walter Gerhard D. H. Kruger Howard Bussey John L. Gerin Edward Kuff Janet Butel Anne A. Gershon Michael Lai Bruce Calnek Mary Jane Gething Ronald A. Laskey Robert B. Carroll Raymond Gilden Paul Lebowitz Eric B. Carstens W. Paul Glezon Phillip Leder Sherwood Casjens Laurie Glimcher Stanley S. Lefkowitz Esther Chang Yosha Gluzman Robert I. Lehrer Robert Chanock Nigel Godson John Lenard Lan Bo Chen Steve Goff Peter Lengyel Craig Cohen Angus Graham Arnold J. Levine Gary H. Cohen Frank L. Graham Michael Levine Charles Cole Harry B. Greenberg Art Levinson Philip Coleman Mark I. Greene Michael Liebowitz Richard Colonno Terry Grodziger Frank Lilly Richard W. Compans Charles F. Grose Tomas Lindahl Jon Condra Ashley T. Haase David Linemeyer Louis Z. Cooper Mary Haffey Maxine Linial Richard J. Courtney Gordon Hager David Livingston Richard L. Crowell Jules Hallum Harvey Lodish Clyde Crumpacker Scott B. Halstead Carlos Lopez J. Lucas-Lenard David Porter Bruce W. Stillman George Mackie Poteete Steven E. Straus Tak Mak Kenneth L. Powell James Strauss Kirstine Mann Carol Prives Jack L.
Recommended publications
  • Purification and Propertiesof a DNA-Binding Protein With
    Proc. Natl. Acad. Sci. USA Vol. 73, No. 7, pp. 2249-2253, July 1976 Biochemistry Purification and properties of a DNA-binding protein with characteristics expected for the Cro protein of bacteriophage X, a repressor essential for lytic growth (bacteriophage X cro gene/promoter-operator DNA) ATIS FOLKMANIS, YOSHINORI TAKEDA, JOSEF SIMUTH, GARY GUSSIN*, AND HARRISON ECHOLS Department of Molecular Biology, University of California, Berkeley, Calif. 94720, and * Department of Zoology, University of Iowa, Iowa City, Iowa 52242 Communicated by A. D. Kaiser, April 14, 1976 ABSTRACT The Cro protein specified by bacteriophage X viously (8), X DNA was labeled with P2p by growth of phage in is a repressor essential for normal lytic growth of the virus, thus low phosphate medium containing 5 ,Ci/ml of UP-labeled having a physiological role distinct from that of cI, the repressor that maintains lyso We have purified a X-specific DNA- inorganic phosphate. Phage were purified by precipitation with binding protein witheny.the requirements for synthesis and bio- polyethylene glycol and centrifugation to equilibrium in a CsCI chemical activities expected for Cro protein from studies in vivo. density gradient (2-3 times). DNA was extracted with redis- As isolated, the protein appears to be a dimer of molecular tilled phenol, the phenol was removed by extraction with ether, weight approximately 18,000 with DNA-binding properties that and the DNA was dialyzed into and stored in 10mM Tris-HCl, are very similar, but not identical, to those of the cI protein. We 0.2 mM EDTA, at pH 7.3. infer that bacteriophage X uses the same regulatory region of DNA for two different DNA-binding repressor proteins with DNA-Binding Assay.
    [Show full text]
  • Pamela L. Mellon, Ph.D
    Pamela L. Mellon, Ph.D. Vice-Chair for Research, Department of Reproductive Medicine Distinguished Professor, Departments of Reproductive Medicine and Neurosciences Director, Center for Reproductive Science and Medicine University of California, San Diego, School of Medicine 3A14 Leichtag Biomedical Research Building 9500 Gilman Drive, La Jolla, CA 92093-0674 (858) 534-1312, Fax (858) 534-1438, e-mail: [email protected] Departmental Web page: http://repromed.ucsd.edu/divisions/endocrinology/mellon.shtml Laboratory Web Page: http://repro.ucsd.edu/Mellon/SitePages/home.aspx ORCID 0000-0002-8856-0410 EDUCATION B.A., 1975, University of California at Santa Cruz Degrees in both Biology and Chemistry with Highest Honors Ph.D., 1979, University of California at Berkeley Department of Molecular Biology Dissertation: Two Transforming Genes and Three Replicative Genes of Avian RNA Tumor Viruses: Identification, Gene Order, and Gene Expression APPOINTMENTS Research Associate, 1975, University of California at Berkeley Department of Molecular Biology with Dr. Harrison Echols Postdoctoral Fellow with Dr. Tom Maniatis 1979-1980, California Institute of Technology, Division of Biology 1980-1984, Harvard University, Department of Biochemistry and Molecular Biology Assistant Professor 1984-1990, The Salk Institute for Biological Studies, Regulatory Biology Laboratory Assistant Adjunct Professor 1988-1991, University of California, San Diego Associate Professor 1990-1991, The Salk Institute for Biological Studies, Regulatory Biology Laboratory Associate
    [Show full text]
  • Journal of Virology
    JOURNAL OF VIROLOGY VOLUME 37 0 NUMBER 1 0 JANUARY 1981 EDITORIAL BOARD Robert R. Wagner, Editor-in-Chief (1982) University of Virginia School of Medicine, Charlottesville Dwight L. Anderson, Editor (1983) Haold S. Ginsberg, Editor (1984) School ofDentistry, Columbia University University of Minnesota, New York, N. Y. Minneapolis David T. Denhardt, Editor (1982) Edward M. Scolnick, Editor (1982) University of Western Ontario National Cancer Institute London, Ontario, Canada Bethesda, Md. David Baltimore (1981) Calderon Howe (1982) Dan S. Ray (1983) Amiya K. Banerjee (1982) Alice S. Huang (1981) M. E. Reichmann (1982) Kenneth I. Berns (1982) Tony Hunter (1983) Bernard E. Reilly (1983) David H. L. Bishop (1982) D. C. Kelly (1982) Wiliam S. Robinson (1983) David Botstein (1982) Thomas J. Kelly, Jr. (1982) Bernard Roizman (1982) Dennis T. Brown (1981) George Khoury (1981) Roland R. Rueckert (1982) Ahmad 1. Bukhari (1981) Jonathan A. King (1981) Norman P. Salzman (1981) Purnell Cboppin (1983) David W. Kingsbury (1982) Joseph Sambrook (1982) John M. Coffin (1983) Daniel Kolakofsky (1983) PrisciUa A. Schaffer (1981) Richard W. Compans (1982) Lloyd M. Kozboff (1982) Sondra Schlesinger (1983) Geoffrey M. Cooper (1981) Robert M. Krug (1983) June R. Scott (1983) Clive Dickson (1981) Robert A. Lazzarini 1981) Phillip A. Sharp (1982) Walter Doerfler (1983) Richard A. Lerner (1981) Aaron J. Shatkin (1982) Harrison Echols (1981) Myron Levine (1982) Saul J. Sllverstein (1982) Elvera Ehrenfeld (1983) Tomas Lindahl (1981) Lee D. Simon (1981) Robert N. Eisenman (1982) Douglas R. Lowy (1983) Kai Simons (1981) Suzanne U. Emerson (1983) Ronald B. Luftig (1981) Patrcia G. Spear (1981) Lynn Enquist (1981) Robert Martin (1981) Mark F.
    [Show full text]
  • Duplication Mutation As an SOS Response in Escherichia Coli
    Copyright 0 1989 by the Genetics Society of America Duplication Mutation as anSOS Response in Escherichia coli: Enhanced Duplication Formationby a Constitutively Activated RecA Joan Dimpfl and Harrison Echols Department of Molecular Biology, University of CaE$ornia, Berkeley, California 94720 Manuscript received March 10, 1989 Accepted for publication July 6, 1989 ABSTRACT The SOS response in Escherichia coli involves the induction of a multioperon regulatory system, which copes withthe presence of DNA lesions that interfere with DNA replication. Induction depends on activation of the RecA protein to cleave the LexA repressor of SOS operons. In addition to inducible DNA repair, the SOS system producesa large increasein the frequency of point mutations. To examine the possibility that other types of mutations are induced as partof the SOS response, we have studied the production of tandem duplications.To avoid the complications of indirect effectsof the DNA lesions, we have activated the SOS response by a constitutive mutation in the recA gene, recA730. The introduction of the recA730 mutation results in an increase in duplications in the range of tenfold or greater, as judged by two different criteria. Based on its genetic requirements, the pathway for induced duplication formation is distinct from the point mutation pathway and also differs from the major normal recombination pathway.The induction of pathways for both duplica- tions and point mutationsshows that the SOS system produces a broad mutagenic response.We have suggested previously that many typesof mutations might be inducedby severe environmental stress, thereby enhancing genetic variationin an endangered population. HE introduction of a replication-inhibitinglesion deletions, translocations) (ECHOLS198 1 ; 1982; Mc- T (by UV light or a chemical mutagen) into the DONALD1984).
    [Show full text]
  • Activity of the Hsp7o Chaperone Complex-Dnak, Dnaj, And
    Proc. Natl. Acad. Sci. USA Vol. 89, pp. 12108-12111, December 1992 Biochemistry Activity of the Hsp7O chaperone complex-DnaK, DnaJ, and GrpE- in initiating phage A DNA replication by sequestering and releasing A P protein (heat shock proteins/DNA replication/protein-protein interaction) HEIDI J. HOFFMANN, SUSAN K. LYMAN, CHI Lu, MARIE-AGNES PETIT, AND HARRISON ECHOLS Division of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720 Contributed by Harrison Echols, September 24, 1992 ABSTRACT Initiation of DNA replication by phage A occurs efficiently with less DnaK, and the unwinding reaction requires the ordered assembly and disassembly ofa specialized is more often bidirectional, indicating a more efficient disas- nucleoprotein structure at the origin of replication. In the sembly reaction (C. Wyman, C. Vasilikiotis, D. Ang, C. disasembly pathway, a set of Escherichia coli heat shock Georgopoulos, and H.E., unpublished work). Based on a proteins termed the Hsp7O complex-DnaK, DnaJ, and variety of data, the three-protein set of heat shock proteins GrpE-act with ATP to release A P protein from the nucleo- appears likely to function typically together. DnaJ and GrpE protein complex, freeing the DnaB helicase for its DNA- markedly stimulate the ATPase activity of DnaK, the bac- unwinding reaction. To investigate the mechanism of the terial homolog ofthe eukaryotic -70-kDa heat shock protein release reaction, we have exmned the interaction between P Hsp7O (14). Moreover, the three-protein set ("Hsp7O com- and the three heat shock proteins by glycerol gradient sedi- plex") acts together in other reactions, including control of mentation and gel electrophoresis.
    [Show full text]
  • Activity of the Purified Mutagenesis Proteins Umuc, Umud', and Reca
    Proc. Natl. Acad. Sci. USA Vol. 89, pp. 10777-10781, November 1992 Biochemistry Activity of the purified mutagenesis proteins UmuC, UmuD', and RecA in replicative bypass of an abasic DNA lesion by DNA polymerase III (SOS respon/fdelity of DNA repfcatlon/umutatlo) MALINI RAJAGOPALANt, CHI Lut, ROGER WOODGATEtt, MIKE O'DONNELL§, MYRON F. GOODMAN$, AND HARRISON ECHOLSt tDivision of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720; 1Department of Microbiology, Cornell University Medical College, New York, NY 10021; and IDepartment of Biological Science, University of Southern California, Los Angeles, CA 90089 Contributed by Harrison Echols, August 17, 1992 ABSTRACT The introduction of a replication-inhibiting SOS mutagenesis (C. Bonner, S. Creighton and M.F.G., lesion Into the DNA ofEscherichia colU generates the Induced, unpublished work). multigene SOS response. One component of the SOS response Together, the studies noted above give clear indications is a marked increase in mutation rate, de t on RecA that SOS mutagenesis is a consequence ofreplicative bypass protein and the induced muta p us UmuC and of DNA lesions mediated by a damage-localized nucleopro- UmuD. A variety of previous indirect ap es have Indi- tein complex involving RecA, UmuC-UmuD', and pol III-a cated that SOS mutagenesi results from replicative bypass of "mutasome" (14, 17). However, direct evidence for such a the DNA lesion by DNA polymerase (pol ) me in pathway has been lacking in the absence of a defined bio- a reaction mediated by RecA, UmuC, and a prcsd form of chemical system. In the work reported here, we have used UmuD termed UmuD'.
    [Show full text]
  • Establishment and Maintenance of Repression by Bacteriophage Lambda: the Role of the Ci, Cit, and Ciii Proteins (E
    Proc. Nat. Acad. Sci. USA Vol. 68, No. 9, pp. 2190-2194, September 1971 Establishment and Maintenance of Repression by Bacteriophage Lambda: The Role of the ci, cit, and ciII Proteins (E. coli/lysogeny versus lysis/cy- mutants/DNA binding) HARRISON ECHOLS AND LINDA GREEN Department of Molecular Biology, University of California, Berkeley, Calif. 94720 Communicated by A. D. Kaiser, July 8, 1971 ABSTRACT To define the events necessary for the provided by the cI protein; for example, an inhibition of establishment and maintenance of repression in a X- of late proteins might delay the late stage of lytic infected cell, we have studied the requirements for efficient synthesis synthesis of the cI protein ("X-repressor"). Three classes development until cl-mediated repression can take over (3). of X mutants defective in the establishment of repression Another plausible mechanism involves timing the estab- are also defective in the appearance of cI protein activity lishment of repression by the time of synthesis of cI protein; at the normal time. Two of these mutational classes (cII- this possibility is suggested by the finding that the syn- and cIII-) probably result from inactivation of X-specified proteins, but the third class (cy-) may involve a structural thesis of cI protein is subject to regulation (4). defect. We conclude that at least three regulatory elements Since active clI and cII genes are essential for the effective are likely to be required for the normal turn-on of cI pro- establishment of lysogeny in an infected cell, but not for the tein synthesis in an infected nonlysogenic cell: clI and maintenance of lysogeny (5), the cII and cIII proteins are cIII proteins and an "active" y-region of X DNA.
    [Show full text]
  • Stabilization of an Origin Complex with Epstein-Barr Nuclear Antigen 1
    Proc. Natl. Acad. Sci. USA Vol. 88, pp. 10870-10874, December 1991 Biochemistry DNA looping between the origin of replication of Epstein-Barr virus and its enhancer site: Stabilization of an origin complex with Epstein-Barr nuclear antigen 1 WEN SU*, TIM MIDDLETONt, BILL SUGDENt, AND HARRISON ECHOLS* *Division of Biochemistry and Molecular Biology, University of California, Berkeley, CA 94720; and tMcArdle Laboratory for Cancer Research, University of Wisconsin, Madison, WI 53706 Contributed by Harrison Echols, September 5, 1991 ABSTRACT Epstein-Barr nuclear antigen 1 (EBNA-1) is transcriptional regulation, recent work has demonstrated the only viral protein required to support replication of Ep- association ofDNA-bound proteins between sites involved in stein-Barr virus during the latent phase of its life cycle. The enhancer function by the bacterial NtrC protein (15), the DNA segment required for latent replication, oriP, contains mammalian Spl protein (16, 17), the viral bovine papilloma two essential binding regions for EBNA-1, termed FR and DS, E2 protein (18), and the Spl and E2 proteins (19). Our work that are separated by 1 kilobase pair. The FR site appears to on EBNA-1 has been directed toward two questions: Does function as a replicational enhancer providing for the start of replicational enhancement involve the protein-protein asso- replication at the DS site. We have used electron microscopy to ciation ofDNA-bound EBNA-1? Why do enhancers typically visualize the interaction of EBNA-1 with its binding sites and act only from relatively close sites on the same DNA mole- to study the mechanism for communication between the FR and cule? DS sites.
    [Show full text]
  • Genetic Map of Bacteriophage Lambda
    MICROBIOLOGICAL REVIEWS, Sept. 1978, p. 577-591 Vol.42, No. 3 0146-0749/78/0042-0577$02.00/0 Copyright © 1978 American Society for Microbiology Printed in U.S.A. Genetic Map of Bacteriophage Lambda HARRISON ECHOLS* AND HELIOS MURIALDO Department ofMolecular Biology, University of California, Berkeley, California 94720, * and Department of Medical Genetics, University of Toronto, Toronto M5S 1A8, Canada INTRODUCTION .5..577 PHYSICAL STATES AND ACTIVITY OF THE A GENOME 577 GENETIC MAP OF THE A GENOME .577 ACTIITrY MAP OF THE A GENOME .583 COMMENTS ON GENETIC ORGANIZATION ...........5*583 LITERATURE CITED .584 INTRODUCTION that are the obligatory precursors for the The study of bacteriophage A has been a cen- cleaved, linear molecules packaged into a phage tral endeavor of molecular biology for a number head (Fig. 1). The lysogenic pathway involves a of years. Phage A has been the creature of choice repression of transcription and a site-specific for many investigators interested in deoxyribo- recombination event that inserts A DNA into nucleic acid (DNA) transcription, replication, the host Escherichia coli genome. This integra- and recombination, in nucleoprotein assembly, tive recombination between the phage and host and in the organization of these processes into attachment sites (att) generates a genetic struc- temporally regulated pathways. As a result of ture that is permuted from the linear order this intensive study, a great deal of information found in the phage particle because the phage is now available about A genes and how they attachment site (a a' or P P) is approximately work; however, the communication of this in the center of the mature DNA molecule (Fig.
    [Show full text]
  • The Cyclical Return of the IQ Controversy: Revisiting the Lessons of the Resolution on Genetics, Race and Intelligence
    Journal of the History of Biology https://doi.org/10.1007/s10739-021-09637-6 ORIGINAL RESEARCH The Cyclical Return of the IQ Controversy: Revisiting the Lessons of the Resolution on Genetics, Race and Intelligence Davide Serpico1 Accepted: 17 April 2021 © The Author(s) 2021 Abstract In 1976, the Genetics Society of America (GSA) published a document enti- tled “Resolution of Genetics, Race, and Intelligence.” This document laid out the Society’s position in the IQ controversy, particularly that on scientifc and ethical questions involving the genetics of intellectual diferences between human popula- tions. Since the GSA was the largest scientifc society of geneticists in the world, many expected the document to be of central importance in settling the controversy. Unfortunately, the Resolution had surprisingly little infuence on the discussion. In 1979, William Provine analyzed the possible factors that decreased the impact of the Resolution, among them scientists’ limited understanding of the relationship between science and ethics. Through the analysis of unpublished versions of the Resolution and exchanges between GSA members, I will suggest that the limited impact of the statement likely depended on a shift in the aims of the GSA due to the controversies that surrounded the preparation of the document. Indeed, the demands of the membership made it progressively more impartial in both scientifc and politi- cal terms, decreasing its potential signifcance for a wider audience. Notably, the troubled history of the Resolution raises the question of what can make efective or inefective the communication between scientists and the public—a question with resonance in past and present discussions on topics of social importance.
    [Show full text]
  • Securities and Exchange Commission Washington, D.C. 20549 ======
    SECURITIES AND EXCHANGE COMMISSION WASHINGTON, D.C. 20549 ================================================================================ (MARK ONE) |X| ANNUAL REPORT UNDER SECTION 13 OR 15(d) OF THE SECURITIES EXCHANGE ACT OF 1934 For the fiscal year ended March 31, 2004 OR |_| TRANSITION REPORT UNDER SECTION 13 OR 15(d) OF THE SECURITIES EXCHANGE ACT OF 1934 For transition period from ________ to __________ Commission file number 0-21846 AETHLON MEDICAL, INC. --------------------- (Name of Small Business issuer in its charter) NEVADA 13-3632859 ------ ---------- (State or other jurisdiction of (I.R.S. Employer incorporation or organization) Identification No.) 7825 FAY AVENUE, SUITE 200, LA JOLLA, CALIFORNIA 92037 -------------------- ----- (Address of principal executive office) (Zip Code) ISSUER'S TELEPHONE NUMBER (858) 456-5777 SECURITIES REGISTERED UNDER SECTION 12(b) OF THE EXCHANGE ACT: NAME OF EACH EXCHANGE TITLE OF EACH CLASS ON WHICH REGISTERED ------------------- ------------------- NONE NONE SECURITIES REGISTERED UNDER SECTION 12(g) OF THE EXCHANGE ACT: COMMON STOCK--$.001 PAR VALUE (TITLE OF CLASS) Check whether the issuer (1) filed all reports required to be filed by Section 13 or 15(d) of the Exchange Act during the past 12 months (or for such shorter period that the registrant was required to file such reports), and (2) has been subject to such filing requirements for the past 90 days. Yes X No _ Check if there is no disclosure of delinquent filers pursuant to Item 405 of Regulation S-B contained in this form, and no disclosure will be contained, to the best of registrant's knowledge, in definitive proxy or information statements incorporated by reference in Part III of this Form 10-KSB or any amendment to this Form 10-KSB.( ) Revenues of the registrant for the fiscal year ended March 31, 2004 were $0.
    [Show full text]
  • Indians, Homesteaders and Molecular Biologists
    Indians, Homesteaders and Molecular Biologists A History of Biochemistry and the Department of Biochemistry & Molecular Biology of the University of Oklahoma Health Sciences Center John R. Sokatch George Lynn Cross Research Professor Emeritus Copyrighted by the Regents of the University of Oklahoma, 2001 Preface The University of Oklahoma Medical School is nearing its 100th anniversary as a separate program of the University and the Department of Biochemistry was founded just over 75 years ago. The science of biochemistry has assumed a central position in all of the biological sciences – even taxonomy. The time has come to document the history of Biochemistry at the Medical School before some of these memories are lost. Much of this history will include histories of Oklahoma, of the Norman campus of the University, politics of Oklahoma, history of the Medical School and some of the big picture of the science of biochemistry because all of these had an impact on the development of the Department. The Medical School began on the Norman Campus where Biochemistry (at that time called Physiological Chemistry) was taught by the Chemistry Department of the University. Paul Weigel suggested the idea for a history of the Department. Without his support this treatise would not have been completed. I had no idea how interesting the project would turn out to be, but maybe Paul did which is why he made the suggestion. I would especially like to thank Joyce Anderson and Paul for their valuable service in editing the manuscript. I would also like to thank Joyce Anderson and Judith Britt who provided the administrative support needed.
    [Show full text]