An inhibitor which interferes with the enzymatic aminoacylation of tRNA |
| |
| Affiliation: | 1. Viral Populations and Pathogenesis Unit, Institut Pasteur, CNRS UMR 3569, 25–28 rue du Dr. Roux, 75724 Paris Cedex 15, France;2. University of Paris Diderot, Sorbonne Paris Cité, Cellule Pasteur, 75013 Paris, France;3. Virologie et Immunologie Moléculaire, INRA, Domaine de Vilvert, 78352 Jouy-en-Josas, France;4. Macrophages et Développement de l’Immunité, Institut Pasteur, 25–28 rue du Dr. Roux, 75724 Paris Cedex 15, France;5. CNRS URA2578, 75724 Paris Cedex 15, France;6. Unité de Génétique Fonctionnelle des Maladies Infectieuses, Institut Pasteur, 25–28 rue du Dr. Roux, 75724 Paris Cedex 15, France;1. Max Planck Institute of Immunobiology and Epigenetics, 79108 Freiburg, Germany;2. The Kennedy Institute of Rheumatology, University of Oxford, Oxford OX3 7FY, UK;3. Department of Immunology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;4. Evergrande Center for Immunologic Diseases, Harvard Medical School and Brigham and Women’s Hospital, Boston, MA 02115, USA;5. Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA;6. Department of Electrical Engineering and Computer Science, University of California, Berkeley, Berkeley, CA 94720, USA;7. Center for Computational Biology, University of California, Berkeley, Berkeley, CA 94720, USA;8. Division of Haematology, University Hospital Zurich and University of Zurich, 8091 Zurich, Switzerland;9. Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany;10. The Bloomberg∼Kimmel Institute for Cancer Immunotherapy at Johns Hopkins, Johns Hopkins University, Baltimore, MD, USA;1. Institute for Biology/Genetics, Freie Universität Berlin, Berlin 14195, Germany;2. NeuroCure Cluster of Excellence, Charité Universitätmedizin Berlin, Berlin 10117, Germany;3. Leibniz-Institut für Analytische Wissenschaften – ISAS – e.V., Dortmund 44139, Germany;4. Department of Chemistry, College of Physical Sciences, University of Aberdeen, Aberdeen AB24 3FX, Scotland, UK;5. Medizinische Fakultät, Medizinische Proteom-Center (MPC), Ruhr-Universität Bochum, Bochum 44801, Germany;6. Department of Chemical Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), 13125 Berlin, Germany;7. Institute of Molecular Biosciences, NAWI Graz, University of Graz, Graz, Austria;8. BioTechMed Graz, Graz, Austria;9. German Centre for Cardiovascular Research (DZHK), partner site Berlin, Berlin 10117, Germany;10. Institute of Pharmacology, Center for Cardiovascular Research, Charité Universitätmedizin Berlin, Berlin 10115, Germany;11. Institute for Mathematics and Computer Sciences, Freie Universität Berlin, Berlin 14195, Germany;12. Zuse Institute Berlin, Berlin 14195, Germany |
| |
| Abstract: | Inactive, frozen and thawed cytoplasmic extracts of 3T3 and SV-101 (3T3 transformed by SV-40 virus) cells contain an inhibitor which blocks the poly(U)-directed incorporation of [14C]phenylalanine into polypeptides, catalyzed by active extracts of these cells. This inhibition is not reversed by adding increased amounts of poly(U). Furthermore, little or no inhibitory activity is observed when poly(U) translation is assayed using precharged [14C]Phe-tRNA. These results suggest that the observed inhibition is not due to the degradation of poly(U) by a nuclease. The inhibitor appears to act primarily at the level of tRNA charging since the synthesis of both Phe-tRNA and Lys-tRNA is impaired in its presence. Evidence is presented which indicates that the inhibitory activity is not due to a high molecular weight protein or nucleic acid. However, the inhibitor appears to be adsorbed to a macromolecule. The inhibitory activity is completely destroyed by ashing. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
