Inhibition of ribosomal translocation by peptidyl transfer ribonucleic acid analogues.
The activity of peptidyl-tRNALys-CpCp2'dA was measured in an in vitro poly(A)-dependent polypeptide synthesizing system derived from Escherichia coli. It has already been shown that Lys-tRNALys-CpCp2'dA is active as an acceptor and Ac2-Lys-tRNALys-Cp2'dA can donate its peptidyl residue but that the overall poly(A)-dependent synthesis of polylysine does not take place with Lys-tRNALys-CpCp2'dA [Wagner, T., Cramer, F., & Sprinzl, M. (1982) Biochemistry 21, 1521-1529]. This is due to the efficient inhibition of the EF-G-dependent translocation of the peptidyl-tRNA CpCp2'dA from the ribosomal A to the ribosomal P site. In addition, the EF-G-dependent release of the deacylated tRNALys-CpCp2'dA from the ribosomes is also inhibited. The action of the elongation factor G or some other ribosomal component participating in the translocation process requires the presence of the 2'-hydroxyl group on the terminal adenosine of tRNA. If this hydroxyl group is not present on the tRNA, the ribosomes remain locked in their pretranslocational state.
D003839:Deoxyadenosines / Q000378:metabolism; D004926:Escherichia coli; D009838:Oligodeoxyribonucleotides / Q000378:metabolism; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism; D011061:Poly A / Q000378:metabolism; D011107:Polylysine / Q000096:biosynthesis; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D003839:Deoxyadenosines; D009838:Oligodeoxyribonucleotides; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D011061:Poly A; D011107:Polylysine; D010444:Peptide Elongation Factor Tu