Covalent cross-linking of AcVal-tRNA to Tetrahymena thermophila cytoplasmic ribosomes and two of its 17S rRNA mutants.
Tetrahymena thermophila 80S ribosomes have been cross-linked to non-enzymatically bound AcVal-tRNA, presumably at the ribosomal P-site. Like the ribosomes from Escherichia coli, yeast, and Artemia salina, cross-linking is exclusively to C-1609, the equivalent of the E. coli C-1400 residue. Mutation of the RNA from G-1707 to A or from U-1711 to C which results in resistance to paromomycin or hygromycin, respectively, failed to affect the rate, yield, or site of cross-linking. The presence of the antibiotics during cross-linking also was without effect. It is concluded that at these two positions the base changes made do not interfere with the tertiary structure of the decoding site.
D000818:Animals; D001483:Base Sequence; D006921:Hygromycin B / Q000494:pharmacology; D008969:Molecular Sequence Data; D009154:Mutation; D010303:Paromomycin / Q000494:pharmacology; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D018894:Reverse Transcriptase Inhibitors; D012270:Ribosomes / Q000378:metabolism*; D013768:Tetrahymena / Q000235:genetics*
D012346:RNA, Transfer, Amino Acyl; D018894:Reverse Transcriptase Inhibitors; C016200:tRNA, N-acetylvaline-; D006921:Hygromycin B; D010303:Paromomycin