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.
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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