Anticodon conformation and accessibility in wild-type and suppressor tryptophan tRNA from E. coli.
The association between Trp-tRNA and Pro-tRNA, which have complementary anticodon sequences, has been used as a probe of anticodon conformation. It is unaffected, however, by the base change in the D-stem present in UGA-suppressor Trp-tRNA. This does not support the hypothesis that UGA suppression depends upon a conformational change induced in the anticodon. The stable denatured form of wild-type Trp-tRNA no longer interacts with Pro-tRNA; the structure of the anticodon region must therefore be quite different in the denatured form.
D000926:Anticodon; D001483:Base Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000032:analysis*; D009690:Nucleic Acid Conformation; D011392:Proline; D012329:RNA, Bacterial / Q000302:isolation & purification; D012343:RNA, Transfer / Q000302:isolation & purification; D014364:Tryptophan
D000926:Anticodon; D012329:RNA, Bacterial; D014364:Tryptophan; D012343:RNA, Transfer; D011392:Proline