Artigo Acesso aberto Revisado por pares

Anticodon conformation and accessibility in wild-type and suppressor tryptophan. tRNA from E.coli.

1976; Oxford University Press; Volume: 3; Issue: 4 Linguagem: Inglês

10.1093/nar/3.4.965

ISSN

1362-4962

Autores

Richard H. Buckingham,

Tópico(s)

Genomics and Phylogenetic Studies

Resumo

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.

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