On the nature of cellular ADP-ribosyltransferase from rat liver specific for elongation factor 2 |
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| Authors: | O Sayhan M Ozdemirli R Nurten E Bermek |
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| Institution: | 2. Biyofizik Bilim Dali, Istanbul Tip Fakültesi çapa , Istanbul, Turkey;1. Research Group of Proteomics and ADP-Ribosylation Signaling, Max Planck Institute for Biology of Ageing, 50931 Cologne, Germany;2. Department of Pharmacology and Chemical Biology, UPMC Hillman Cancer Center, University of Pittsburgh, Pittsburgh, PA, USA;3. Univ Rennes, CNRS, IGDR (Institut de Génétique et Développement de Rennes) – UMR 6290, BIOSIT (Biologie, Santé, Innovation Technologique de Rennes) – UMS 3480, US 018, 35000 Rennes, France;4. Laboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, Biological Research Centre, Eötvös Loránd Research Network (ELKH), 6276 Szeged, Hungary;5. Doctoral School of Multidisciplinary Medical Sciences, University of Szeged, 6276 Szeged, Hungary;6. Department of Immunology, Albert Szent-Györgyi Medical School, Faculty of Science and Informatics, University of Szeged, 6720 Szeged, Hungary;7. Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK;8. Institut Universitaire de France, Paris, France;9. Cologne Excellence Cluster for Stress Responses in Ageing-Associated Diseases (CECAD), University of Cologne, 50931 Cologne, Germany;1. Sir William Dunn School of Pathology, University of Oxford, Oxford, UK;2. Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia;3. School of Biosciences, University of Sheffield, Sheffield, UK;4. Department of Biology, University of Oxford, Oxford, UK;1. Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia;2. Sir William Dunn School of Pathology, University of Oxford, UK |
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| Abstract: | A cellular ADP-ribosyltransferase, specific for elongation factor 2 (EF-2), is found in extracts from rat liver. Co-migrating with EF-2 throughout purification, this activity is, moreover, located in the protein bands corresponding to EF-2 after native or sodium dodecyl sulfate polyacrylamide gel electrophoresis. The observed activity is thus implicated to be an inherent property of EF-2. Preincubation of EF-2 with GuoPPCH2Pox inhibits endogenous, but not diphtheria toxin catalyzed ADP-ribosylation. |
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