Methylglyoxal bis(guanylhydrazone) elimination of polyamine effects on protein synthesis |
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| Authors: | R Ohnishi R Nagami S Hirose K Igarashi |
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| Institution: | 1. Department of Oral and Maxillofacial Pathology, Radiology and Medicine, New York University College of Dentistry, New York, NY 10010, USA;2. Basic and Clinical Neuroscience, Institute of Psychiatry, Psychology and Neuroscience, King''s College London, London, UK;1. Division of Psychology and Mental Health, The University of Manchester, UK;2. Greater Manchester Mental Health NHS Foundation Trust, UK;3. Department of Neurology, Belfast Health and Social Care Trust, Belfast, UK;4. Division of Neuroscience and Experimental Psychology Science, The University of Manchester, UK;5. Royal Manchester Children''s Hospital, Manchester Academic Health Sciences, Manchester, UK |
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| Abstract: | The effect of methylglyoxal bis(guanylhydrazone) (MGBG), a structural analog of polyamines, on protein synthesis has been studied in the presence and absence of spermidine. The spermidine stimulation of polyphenylalanine- and MS2 RNA-directed RNA replicase synthesis in an Escherichia coli cell-free system and of globin synthesis in a rabbit reticulocyte cell-free system disappeared with the addition of MGBG. The spermidine reduction of misincorporation of leucine during polyphenylalanine synthesis in both E. coli and wheat germ cell-free systems was also disturbed by MGBG. MGBG noncompetitively interfered with polyamine stimulation of polyphenylalanine and globin synthesis, suggesting that MGBG could bind to both RNA and the complex of RNA and polyamine. MGBG was preferentially bound to ribosomal RNA among ribosomal RNA, poly(U), and calf thymus DNA, and strongly inhibited the amount of polyamine bound to ribosomal RNA. These results suggest that MGBG elimination of polyamine effects on protein synthesis may occur through the disturbance of polyamine binding to ribosomal RNA. |
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