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The Symposia, 1933 — 2003

1963:   Synthesis and Structure of Macromolecules, Vol. XXVIII

Organizer: H. Edwin Umbarger


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Foreword    v

List of Previous Volumes    vii

Photographs of Some Symposium Participants    viil

List of Those Attending the Symposium    x

Francis J. Ryan    xx


RIS, H. and B. L. CHANDLER. The Ultrastructure of Genetic Systems in Prokaryotes and Eukaryotes

RICHARDSON, C. C., C. L. SCHILDKRAUT and A. KORNBERG. Studies on the Replication of DNA by DNA Polymerases     9

BOLLUM, F. J. Studies on the Nature of Calf Thymus DNA-Polymerase Products     21

BURTON, K., M. R. LUNT, G. B. PETERSEN, and J. C. SIEBKE. Studies of Nucleotide Sequences in DNA     27

MOSIG, G. Genetic Recombination in Bacteriophage T4 During Replication of DNA Fragments     35

CAIRNS, J. The Chromosome of Escherichia coli    43

SUEOKA, N., and H. YOSHIKAWA. Regulation of Chromosome Replication in Bacillus subtilis 4.    47

NAGATA, T. The Sequential Replication of E. coli DNA    55


HURWITZ, J., A. EVANS, C. BABINET, and A. SKALKA. On the Copying of DNA in the RNA Polymerase Reaction     59

CHAMBERLIN, M., and P. BERG. Studies on DNA Directed RNA Polymerase; Formation of DNA-RNA Complexes with Single Stranded f X 174 DNA as Template     67

SPENCER, M. X-Ray Diffraction Studies of the Secondary Structure of RNA     77

FRESCO, J. R., L. C. KLOTZ, and E. G. RICHARDS. A new Spectroscopic Approach to the Determination of Helical Secondary Structure in Ribonucleic Acid    83

HASELKORN, R. Actinomycin D as a Probe for Nucleic Acid Secondary Structure     91

AUGUST, J. T., S. COOPER, L. SHAPIRO, and N. D. ZINDER. RNA Phage Induced RNA Polymerase     95

WEISSMANN, C., L. SIMON, P. BORST, and S. OCHOA. Induction of RNA Synthetase in E. coli After Infection by the RNA Phage, MS 2    99

BALTIMORE, D., and R. M. FRANKLIN. Properties of the Mengovirus and Poliovirus RNA Polymerases l"    105

SPIEGELMAN, S., and R. H. Dol. Replication and Translation of RNA Genomes     109


HOLLEY, R. W., J. APGAR, G. A. EVERETT, J. T. MADISON, S. H. MERRILL, and A. ZAMIR. Chemistry of Amino Acid-Specific Ribonucleic Acids    117

CANTONI, G. L., H. ISHIKURA, H. H. RICHARDS, and K. TANAKA. Studies on Soluble Ribonucleic Acid. XI. A Model for the Base Sequence of Serine S-RNA `%    123

INGRAM, V. M. and J. A. SJOQUIST. Studies on the Structure of Purified Alanine and Valine Transfer RNA from Yeast     133

BOREK, E. The Methylation of Transfer RNA: Mechanism and Function    139

GOLD, M., and J. HURWITZ. The Enzymatic Methylation of the Nucleic Acids     149

LITTAUER, U. Z., K. MUENCH, P. BERG, W. GILBERT, and P. F. SPAHR. Studies on Methylated Bases in Transfer RNA     157


SPIEGELMAN, S., and M. HAYASHI. The Present Status of the Transfer of Genetic Information and Its Control     161

LEVINTHAL, C., D. P. FAN, A. RIGA, and R. A. ZIMMERMAN. The Decay and Protection of Messenger RNA in Bacteria

MARMUR, J., C. M. GREENSPAN, E. PALECEK, F. M. KAHAN, J. LEVINE, and M. MANDEL. Specificity of the Complementary RNA formed by B. subtilis Infected with Bacteriophage SP8     191

HALL, B. D., M. H. GREEN, A. P. NYGAARD, and J. A. BOEZI. Copying of DNA in T2 Infected E.coli 201

BAUTZ, E. K. F. The Structure of T4 Messenger RNA in Relation to Messenger Function    205

DARNELL, J. E., S. PENMAN, K. SCHERRER, and Y. BECKER. A Description of Various Classes of RNA from Hela Cells    183


HARDESTY, B., R. ARLINGHAUS, J. SHAEFFER, and R. SCHWEET. Hemoglobin and Polyphenylanine Synthesis with Reticulocyte Ribosomes. 215

MARKS, P. A., E. R. BURKA, R. RIFKIND, and D. DANON. Polyribosomes Active in Reticulocyte Protein Synthesis    223

NAKAMOTO, T., T. W. CONWAY, J. E. ALLENDE, G. J. SPYRIDES, and F. LIPMANN. Formation of Peptide Bonds I. Peptide Formation from Aminoacyl-S-RNA     227

BENNETT, T. P., J. GOLDSTEIN, and F. LIPMANN. Formation of Peptide Bonds II. Coding Properties of Leucyl-S-RNAs     233

WOOD, W. B., and P. BERG. Studies on the "Messenger" Activity of RNA Synthesized with RNA Polymerase     237

ALLFREY, V. G., and A. E. MIRSKY. Mechanisms of Synthesis and Control of Protein and Ribonucleic Acid Synthesis in the Cell Nucleus    247

MACH, B. The Biosynthesis of an Antibiotic Polypeptide, as Distinguished from Protein Biosynthesis     263

SPIRIN, A. S. In Vitro Formation of Ribosome-like Particles from CM Particles and Protein    267


RICH, A., J. R. WARNER, and H. M. GOODMAN. The Structure and Function of Polyribosomes     269

GILBERT,W.Protein Synthesis in E.coli     287

GROS, F., J. M. DUBERT, A. TISSIERES, S. BOURGEOIS, M. MICHELSON, R. SOFFER, and L. LEGAULT. Regulation of Metabolic Breakdown and Synthesis of Messenger RNA in Bacteria    299

NOMURA,M.Mode of Action of Colicines     315

KEPES, A. Kinetic Analysis of the Early Events in Induced Enzyme Synthesis     325


JACOB, F., S. BRENNER, and F. CUZIN. On the Regulation of DNA Replication in Bacteria    329

AMES,B.N.,andP.E.HARTMAN.The Histidine Operon     349

MARTIN, R. G. The One Operon-One Messenger Theory of Transcription     357

ATTARDI, G., S. NAONO, J. ROUVIERE, F. JACOB, and F. GROS. Production of Messenger RNA and Regulation of Protein Synthesis     363

GUTTMAN, B., and A. NOVICK. A Messenger RNA for b-Galactosidase in E. coli     373

EPSTEIN, R. H., A. BOLLE, C. M. STEINBERG, E. KELLENBERGER, E. BOY, DE LA TOUR, R. CHEVALLEY, R. S. EDGAR, M. SUSMAN, G. DENHARDT, and A. LEILAUSIS. Physiological Studies of Conditional Lethal Mutations of Bacteriophage T4 D     375

THOMAS, C. A. The Arrangements of Nucleotide Sequences in T2 and T5 DNA Molecules     395

N0VICK, A., E. S. LENNOX, and F. JACOB. Relationship Between Rate of Enzyme Synthesis and Repressor Level     397

REVEL, H., and S. E. LURIA. On the Mechanism of Unrepressed Galactosidase Synthesis Controlled by a Transducing Phage    403

SCHACHMAN, H. K. Considerations on the Tertiary Structure of Proteins     409

ZABIN, I.Proteins of the Lactose System     431

BACON, D., and H. J. VOGEL. A Regulatory Gene Simultaneously Involved in Repression and Induction     437


EPSTEIN, C. J., R. F. GOLDBERGER, and C. B. ANFINSEN. Genetic Control of Tertiary Protein Structure: Studies with Model Systems     439

MUIRHEAD, H., and M. F. PERUTZ. Structure of Reduced Human Hemoglobin     451


TOMKINS, G. M., K. L. YIELDING, N. TALAL, andJ. F. CURRAN. Protein Structure and Biological Regulation     461KOSHLAND, D. E., JR. The Role of Flexibility in Enzyme Action    473

WYMAN, J. Allosteric Effects in Hemoglobin     483

GERHART, J. C., and A. B. PARDEE. The Effect of the Feedback Inhibitor, CTP, on Subunit Interactions in Aspartate Transcarbamylase     491

CHANGEUX, J. P. Allosteric Interactions on Biosynthetic L-Threonine Deaminase from E.coli K-12 497FREUNDLICH, M., and H. E. UMBARGER. The Effects of Analogues of Threonine and of Isoleucine on the Properties of Threonine Deaminase     505

COHEN, G. N., and J. C. PATTE. Some Aspects of the Regulation of Amino Acid Biosynthesis in a Branched Pathway     513


FINCHAM, J. R. S., and A. CODDINGTON. The Mechanism of Complementation between am Mutants of Neurospora crassa     517

PERRIN, D. Complementation between Products of the beta-Galactosidase Structural Gene of E. coli     529

ZIPSER, D., and D. PERRIN. Complementation on Ribosomes     533

SCHLESINGER, M. J., A. TORRIANI, and C. LEVINTHAL. In Vitro Formation of Enzymatically Active Hybrid Proteins from E. coli Alkaline Phosphatase CRM's     539

GROSS, S. R., and R. E. WEBSTER. Some Aspects of Interallelic Complementation Involving Leucine Biosynthetic Enzymes of Neurospora     543


NIRENBERG, M. W., O. W. JONES, P. LEDER, B. F. C. CLARK, W. S. SLY, and S. PESTKA. On the Coding of Genetic Information    549

PEYER, J. F., P. LENGYEL, C. BASILIO, A. J. WAHBA, R. S. GARDNER, and S. OCHOA. Synthetic Polynucleotides and the Amino Acid Code    559

YAMANE, T., T. Y. CHENG, and N. SUEOKA. Species Specificity of Amino Acid Transfer-RNA and Amino Acyl-T-RNA Synthetase    569

WEINSTEIN, I. B. Comparative Studies on the Genetic Code    579


YANOFSKY , C. Amino Acid Replacements Associated with Mutation and Recombination in the A Gene and Their Relationship to In Vitro Coding Data      581

WITTMANN, H. G., and B. WITTMANN-LIEBOLD. Tobacco Mosaic Virus Mutants and the Genetic Coding Problem     589


Centers of scientific research are what people choose to make them. This is especially true for the Laboratory at Cold Spring Harbor, which has achieved its scientific reputation not by some happy accident but as the result of the careful guidance of its loyal friends. A few of these friends have at some time worked here for long periods. Others have been regular summer visitors. And others, though never here for very long, have yet shown themselves ready to forsake their own affairs on behalf of the Laboratory in times of need.

This last year saw the withdrawal of the Carnegie Institution of Washington from Cold Spring Harbor and the creation of anew organization "The Cold Spring Harbor Laboratory of Quantitative Biology" to control the entire enterprise. Many people have labored to make the transition possible and so ensure the continued survival of the laboratories. No one worked harder at this than Francis Ryan.

Despite his responsibilities as Chairman of the Department of Zoology at Columbia University, he joined with Dr. Edward L. Tatum and Dr. Rollin D. Hotchkiss in carrying out the early negotiations with the Long Island Biological Association and the Carnegie Institution. Later he became one of the most active of the group of Trustees formed to watch over the new Laboratory at Cold Spring Harbor. In this role, he was ready at all times to give his selfless support and counsel, and to exercise his great powers of gentle persuasion.

Francis Ryan died suddenly, one month after the end of this symposium.The news of his death had the unbelievable quality that comes with the death of a friend. Time will soften this blow, but it will not lessen the great contribution he made to science-through his own research, through the work he inspired in others, and through his great influence on the course of events during a most critical period in the affairs of the laboratory at Cold Spring Harbor. He was 47 at the time of his death.