Analysis of modification-dependent structural alterations in the anticodon loop of Escherichia coli tRNAArg and their effects on the translation of MS2 RNA.
The conformation of the anticodon loop of Escherichia coli tRNAArg was investigated. It is shown that the structure of the anticodon loop is influenced by the base composition of the anticodon stem, and the natural modification of the nucleoside residue 32 in the anticodon loop. The structural effects detected by analysis of the accessibility of the anticodon loop to nuclease S1 could be correlated with the ability of different Arg-tRNAArg species to suppress frame-shifting during translation of MS2 RNA.
D000926:Anticodon / Q000502:physiology*; D003090:Coliphages / Q000235:genetics*; D003562:Cytidine / Q000031:analogs & derivatives; D004720:Endonucleases; D004926:Escherichia coli / Q000235:genetics*; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000502:physiology*; D012346:RNA, Transfer, Amino Acyl; D012367:RNA, Viral / Q000502:physiology*; D015719:Single-Strand Specific DNA and RNA Endonucleases
D000926:Anticodon; D012346:RNA, Transfer, Amino Acyl; D012367:RNA, Viral; C002908:2-thiocytidine; D003562:Cytidine; D012343:RNA, Transfer; D004720:Endonucleases; D015719:Single-Strand Specific DNA and RNA Endonucleases