The extension of polyphenylalanine and polylysine peptides on Escherichia coli ribosomes.
Fluorescence techniques were used to examine aminoacyl-tRNA binding to Escherichia coli ribosomes and the subsequent extension of polyphenylalanine and polylysine nascent peptides. The results demonstrate that deacylated tRNA, an analogue of peptidyl-tRNA and puromycin (an analogue of aminoacyl-tRNA) can be bound simultaneously to the same ribosome. Moreover, the fluorescence properties of nascent polyphenylalanine and polylysine peptides with a fluorophore attached to their amino termini were determined and found to be quite different. This difference is reflected in the effects that erythromycin has in each case.
Department of Chemistry and Biochemistry, University of Texas, Austin 78712.
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D001665:Binding Sites; D004917:Erythromycin / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects; D010455:Peptides; D010458:Peptidyl Transferases / Q000378:metabolism; D011107:Polylysine / Q000096:biosynthesis*; D011691:Puromycin / Q000378:metabolism / Q000494:pharmacology; D012360:RNA, Transfer, Phe / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D010455:Peptides; D012360:RNA, Transfer, Phe; D011107:Polylysine; C012001:polyphenylalanine; D011691:Puromycin; D004917:Erythromycin; D010458:Peptidyl Transferases