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  • Kinetics  (158)
  • American Association for the Advancement of Science (AAAS)  (158)
  • American Chemical Society
  • 2020-2024
  • 1985-1989  (158)
  • 1955-1959
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  • 1
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    The anticodon contains a major element of the identity of arginine transfer RNAs (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: The contribution of the anticodon to the discrimination between cognate and noncognate tRNAs by Escherichia coli Arg-tRNA synthetase has been investigated by in vitro synthesis and aminoacylation of elongator methionine tRNA (tRNA(mMet) mutants. Substitution of the Arg anticodon CCG for the Met anticodon CAU leads to a dramatic increase in Arg acceptance by tRNA(mMet). A nucleotide (A20) previously identified by others in the dihydrouridine loop of tRNA(Arg)s makes a smaller contribution to the conversion of tRNA(mMet) identity from Met to Arg. The combined anticodon and dihydrouridine loop mutations yield a tRNA(mMet) derivative that is aminoacylated with near-normal kinetics by the Arg-tRNA synthetase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulman, L H -- Pelka, H -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1595-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, NY 10461.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2688091" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/*genetics ; Arginine-tRNA Ligase/metabolism ; Base Sequence ; Escherichia coli/enzymology/genetics ; Kinetics ; Methionine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Transfer/*genetics ; RNA, Transfer, Amino Acid-Specific/*genetics ; RNA, Transfer, Arg/*genetics ; Substrate Specificity ; T-Phages/genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Specific interactions in RNA enzyme-substrate complexes (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: Analysis of crosslinked complexes of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli, and transfer RNA precursor substrates has led to the identification of regions in the enzyme and in the substrate that are in close physical proximity to each other. The nucleotide in M1 RNA, residue C92, which participates in a crosslink with the substrate was deleted and the resulting mutant M1 RNA was shown to cleave substrates lacking the 3' terminal CCAUCA sequence at sites several nucleotides away from the normal site of cleavage. The presence or absence of the 3' terminal CCAUCA sequence in transfer RNA precursor substrates markedly affects the way in which these substrates interact with the catalytic RNA in the enzyme-substrate complex. The contacts between wild-type M1 RNA and its substrate are in a region that resembles part of the transfer RNA "E" (exit) site in 23S ribosomal RNA. These data demonstrate that in RNA's with very different cellular functions, there are domains with similar structural and functional properties and that there is a nucleotide in M1 RNA that affects the site of cleavage by the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerrier-Takada, C -- Lumelsky, N -- Altman, S -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1578-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, New Haven, CT 06520.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2480641" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Endoribonucleases/genetics/*metabolism ; Escherichia coli/enzymology/*genetics ; *Escherichia coli Proteins ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/genetics ; RNA, Bacterial/*genetics/metabolism ; RNA, Transfer/genetics ; Ribonuclease P ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Steroid binding at sigma-"opioid" receptors (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarz, S -- Pohl, P -- Zhou, G Z -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1635-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2556797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Brain/metabolism ; Kinetics ; Ligands ; Lymphocytes/metabolism ; Progesterone/blood/cerebrospinal fluid/metabolism ; Receptors, Opioid/*metabolism ; Receptors, sigma ; Steroids/*metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: Rana esculenta tropomyosin assembles in vivo into a coiled-coil alpha helix from two different subunits, alpha and beta, which are present in about equal concentrations. Although the native composition is alpha beta, a mixture of equal amounts of alpha alpha and beta beta is produced by refolding dissociated alpha and beta at low temperature in vitro. Refolding kinetics showed that alpha alpha formed first and was relatively stable with regard to chain exchange below approximately 20 degrees C. Equilibration of the homodimer mixture at 30 degrees and 34 degrees C for long times, however, resulted in the formation of the native alpha beta molecule by chain exchange. Biosynthesis of alpha beta from separate alpha and beta genes is, therefore, favored thermodynamically over the formation of homodimers, and biological factors need not be invoked to explain the preferred native alpha beta composition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehrer, S S -- Qian, Y D -- Hvidt, S -- HL22461/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):926-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Muscle Research, Boston Biomedical Research Institute, MA 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Kinetics ; Macromolecular Substances ; Muscle, Smooth/metabolism ; Muscles/metabolism ; Myocardium/metabolism ; Protein Conformation ; Protein Denaturation ; Protein Processing, Post-Translational ; Rana esculenta ; Thermodynamics ; Tropomyosin/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Inhibition of a class C beta-lactamase by a specific phosphonate monoester (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: A phosphonate monoester, m-carboxyphenyl phenylacetamidomethylphosphonate, has been found to be a specific inhibitor of the class C beta-lactamase of Enterobacter cloacae P99. Inactivation is rapid (10(3) per second per molar concentration) and reactivation very slow (2.2 X 10(-6) per second). Apparently concerted with the inactivation, one equivalent (with respect to the enzyme) of m-hydroxybenzoate is released. Reactivation is accelerated by hydroxylamine and benzohydroxamate. This suggests that the loss of enzyme activity is due to phosphonylation of an active site functional group. This discovery holds the promise of a new general class of beta-lactamase inhibitors and, perhaps, antibiotics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pratt, R F -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):917-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemistry Department, Wesleyan University, Middletown, CT 06457.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814513" target="_blank"〉PubMed〈/a〉
    Keywords: Enterobacter/*enzymology ; Enterobacteriaceae/*enzymology ; Hydroxamic Acids/pharmacology ; Hydroxylamine ; Hydroxylamines/pharmacology ; Kinetics ; Organophosphorus Compounds/*pharmacology ; Protein Binding ; *beta-Lactamase Inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Identification of an AUUUA-specific messenger RNA binding protein (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: An important control point in gene expression is at the level of messenger RNA (mRNA) stability. The mRNAs of certain regulatory cellular proteins such as oncogenes, cytokines, lymphokines, and transcriptional activators are extremely labile. These messages share a common AUUUA pentamer in their 3' untranslated region, which confers cytoplasmic instability. A cytosolic protein was identified that binds specifically to RNA molecules containing four reiterations of the AUUUA structural element. This protein consists of three subunits and binds rapidly to AUUUA-containing RNA. Such protein-RNA complexes are resistant to the actions of denaturing and reducing agents, demonstrating very stable binding. The time course, stability, and specificity of the protein-AUUUA interaction suggests the possibility that the formation of this complex may target susceptible mRNA for rapid cytoplasmic degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malter, J S -- CA01427-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):664-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Tulane University School of Medicine, New Orleans, LA 70112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814487" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding, Competitive ; Carrier Proteins/isolation & purification/*metabolism ; Cell Line ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Weight ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/*metabolism ; *RNA-Binding Proteins ; Ribonuclease, Pancreatic
    Print ISSN: 0036-8075
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  • 7
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    Proton motive force involved in protein transport across the outer membrane of Aeromonas salmonicida (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: Many Gram-negative bacteria export proteins to the exterior. Some of these proteins are first secreted into the periplasm and then cross the outer membrane in a separate step. The source of energy required for the translocation is unknown. Export of the extracellular protein proaerolysin from the periplasm through the outer membrane of Aeromonas salmonicida is inhibited by a proton ionophore and by low extracellular pH. One possible explanation of these results is that a proton gradient across the outer membrane is required for export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, K R -- Buckley, J T -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):654-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814486" target="_blank"〉PubMed〈/a〉
    Keywords: Aeromonas/drug effects/*metabolism ; Bacterial Toxins/*metabolism ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Cell Membrane/metabolism ; Culture Media ; Hemolysin Proteins/*metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Pore Forming Cytotoxic Proteins
    Print ISSN: 0036-8075
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  • 8
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    Dispersed polaron simulations of electron transfer in photosynthetic reaction centers (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-10-06
    Description: A microscopic method for simulating quantum mechanical, nuclear tunneling effects in biological electron transfer reactions is presented and applied to several electron transfer steps in photosynthetic bacterial reaction centers. In this "dispersed polaron" method the fluctuations of the protein and the electron carriers are projected as effective normal modes onto an appropriate reaction coordinate and used to evaluate the quantum mechanical rate constant. The simulations, based on the crystallographic structure of the reaction center from Rhodopseudomonas viridis, focus on electron transfer from a bacteriopheophytin to a quinone and the subsequent back-reaction. The rates of both of these reactions are almost independent of temperature or even increase with decreasing temperature. The simulations reproduce this unusual temperature dependence in a qualitative way, without the use of adjustable parameters for the protein's Franck-Condon factors. The observed dependence of the back-reaction on the free energy of the reaction also is reproduced, including the special behavior in the "inverted region."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warshel, A -- Chu, Z T -- Parson, W W -- GM-40283/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Oct 6;246(4926):112-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Southern California, Los Angeles 90007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2675313" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; *Electron Transport ; Kinetics ; Models, Chemical ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins ; Rhodopseudomonas/metabolism ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-09-15
    Description: The neutrophil Mac-1 and gp100MEL-14 adhesion proteins are involved in neutrophil extravasation during inflammation. Both the expression and activity of Mac-1 are greatly increased after neutrophil activation. In contrast, neutrophils shed gp100MEL-14 from the cell surface within 4 minutes after activation with chemotactic factors or phorbol esters, releasing a 96-kilodalton fragment of the antigen into the supernatant. Immunohistology showed that gp100MEL-14 was downregulated on neutrophils that had extravasated into inflamed tissue. The gp100MEL-14 adhesion protein may participate in the binding of unactivated neutrophils to the endothelium; rapid shedding of gp100MEL-14 may prevent extravasation into and damage of normal tissues by activated neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kishimoto, T K -- Jutila, M A -- Berg, E L -- Butcher, E C -- AI 19957/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Sep 15;245(4923):1238-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2551036" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation/*immunology ; Antigens, Surface/*immunology ; Bone Marrow Cells ; Cell Adhesion ; Cell Adhesion Molecules ; Chemotactic Factors/*physiology ; Complement C5/physiology ; Complement C5a ; Fluorescent Antibody Technique ; Interleukin-1/physiology ; Interleukin-8 ; Kinetics ; Leukotriene B4/physiology ; Lipopolysaccharides/physiology ; Lymphocyte Activation ; Macrophage Activation ; Macrophage-1 Antigen ; Mice ; Mice, Inbred BALB C ; Neutrophils/cytology/*immunology ; Tetradecanoylphorbol Acetate ; Tumor Necrosis Factor-alpha/physiology
    Print ISSN: 0036-8075
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  • 10
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    Synthesis of functional human hemoglobin in transgenic mice (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-09-01
    Description: Human alpha- and beta-globin genes were separately fused downstream of two erythroid-specific deoxyribonuclease (DNase) I super-hypersensitive sites that are normally located 50 kilobases upstream of the human beta-globin gene. These two constructs were coinjected into fertilized mouse eggs, and expression was analyzed in transgenic animals that developed. Mice that had intact copies of the transgenes expressed high levels of correctly initiated human alpha- and beta-globin messenger RNA specifically in erythroid tissue. An authentic human hemoglobin was formed in adult erythrocytes that when purified had an oxygen equilibrium curve identical to the curve of native human hemoglobin A (Hb A). Thus, functional human hemoglobin can be synthesized in transgenic mice. This provides a foundation for production of mouse models of human hemoglobinopathies such as sickle cell disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behringer, R R -- Ryan, T M -- Reilly, M P -- Asakura, T -- Palmiter, R D -- Brinster, R L -- Townes, T M -- HD-09172/HD/NICHD NIH HHS/ -- HL-35559/HL/NHLBI NIH HHS/ -- HL-38632/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Sep 1;245(4921):971-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Reproductive Physiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2772649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Deoxyribonuclease I ; Female ; *Genes ; Globins/biosynthesis/*genetics ; Hemoglobins/biosynthesis/*genetics ; Humans ; Kinetics ; Mice ; Mice, Transgenic ; Oxyhemoglobins/metabolism ; RNA, Messenger/genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
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