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Title: [Interaction of dansyl-dipeptidyl-tRNA with E. coli ribosomes]. Author: Vigestane RIa, Aleksandrova LA, Strel'tsov SA, Viktorova LS, Kukhanova MK. Journal: Biokhimiia; 1976 Sep; 41(9):1641-5. PubMed ID: 788800. Abstract: Dansyl-dipeptidyl-tRNA is found to bind with ribosomes in the presence of polyU much more efficiently than AcPhe-tRNA. 30-80% OF introduced danysl-dipeptidyl-tRNA is in a complex with ribosomes and reacts with puromycin in the presence of 5 mM Mg2+. A significant binding of dansyl-dipeptidyl-tRNA both for acceptor and donor ribosome regions is observed in the presence of 10 mMg2+, unlike AcPhe-tRNA, which is capable of the binding only at 20 mM Mg2+. A peptide transfer from dansyl-dipeptidyl-tRNA on puromycin takes place at 10 mM Mg2+ in the absence of template, while AcPhe-tRNA efficiently interacts with puromycin only at 20 mM Mg2+. The data obtained suggest that the increase of hydrophobity of a peptide residue in peptidyl-tRNA increases its binding in peptidyl transferase of ribosomes.[Abstract] [Full Text] [Related] [New Search]