The human large subunit ribosomal protein L36A-like contacts the CCA end of P-site bound tRNA |
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| Authors: | Soria Baouz Anne Woisard Sylvie Sinapah Jean-Pierre Le Caer Manuela Argentini Konstantin Bulygin Gustave Aguié Codjo Hountondji |
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| Institution: | 2. CNRS-UPR 2301, Institut de Chimie des Substances Naturelles (ICSN), Avenue de la Terrasse, F-91198 Gif-Sur-Yvette, France;3. Institute of Chemical Biology and Fundamental Medecine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, 630090 Novosibirsk, Russia;1. Division of General Surgery, Rutgers–Robert Wood Johnson Medical School, New Brunswick, NJ;2. Mount Sinai Hospital, New York, NY;3. St. Lukes Health Network in Bethlehem, PA;4. Rutgers Cancer Institute of New Jersey, New Brunswick, NJ;5. Department of Pathology, Rutgers-Robert Wood Johnson Medical School, New Brunswick, NJ;1. Haemato-Oncology Research Unit, Division of Molecular Pathology, Division of Cancer Biology, The Institute of Cancer Research, Sutton SM2 5NG, UK;1. Centre for Experimental Research and Medical Studies (CERMS), Azienda Ospedaliera Universitaria Città della Salute e della Scienza di Torino, Turin, Italy;2. Immunogenetic and Transplant Biology Service, Azienda Ospedaliera Universitaria Città della Salute e della Scienza di Torino, Turin, Italy;3. Department of Experimental and Clinical Medicine, University of Florence, Florence, Italy;4. Department of Biomedicine, Azienda Ospedaliera Universitaria Careggi (AOUC), Florence, Italy;5. Department of Molecular Biotechnology and Health Sciences, University of Turin, Turin, Italy;6. SCDU Epidemiologia dei Tumori-CPO Piemonte, Azienda Ospedaliera Universitaria Città della Salute e della Scienza di Torino, Turin, Italy;7. BioClarma, Molecular Biotechnology Centre, Turin, Italy;8. Department of Medical Sciences, University of Turin, Turin, Italy;9. Tumor Immunology Unit, IRCCS-San Raffaele Scientific Institute, Milan, Italy;10. Proteome Biochemistry, IRCCS-San Raffaele Scientific Institute, Milan, Italy;11. Molecular Biotechnology Center, University of Turin, Turin, Italy |
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| Abstract: | Periodate-oxidized tRNA (tRNAox), the 2′,3′-dialdehyde derivative of tRNA, was used as a zero-length active site-directed affinity labeling reagent, to covalently label proteins at the binding site for the 3′-end of tRNA on human 80S ribosomes. When human 80S ribosomes were reacted with tRNAAspox positioned at the P-site, in the presence of an appropriate 12 mer mRNA, a set of two tRNAox-labeled ribosomal proteins (rPs) was observed. The majorily labeled protein was identified as the large subunit rP L36a-like (RPL36AL) by means of mass spectrometry. Intact tRNAAsp competed with tRNAAspox for the binding to the P-site, by preventing tRNA-protein cross-linking with RPL36AL. Altogether, the data presented in this report are consistent with the presence of RPL36AL at or near the binding site for the CCA end of the tRNA substrate positioned at the P-site of human 80S ribosomes. It is the first time that a ribosomal protein is found in an intimate contact (i.e. at a zero-distance) with a nucleotide of the conserved CCA terminus of P-site tRNA which is the substrate of peptidyl transferase reaction. RPL36AL which is strongly conserved in eukaryotes belongs to the L44e family of rPs, a representative of which is Haloarcula marismortui RPL44e. |
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