Aminoacyl-tRNA synthetase-induced cleavage of tRNA.
AUTOR(ES)
Beresten, S
RESUMO
Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNA(Gln) species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=312233Documentos Relacionados
- Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates
- Aminoacylation of tRNA in the evolution of an aminoacyl-tRNA synthetase
- A truncated aminoacyl–tRNA synthetase modifies RNA
- The aminoacyl-tRNA Synthetase Data Bank (AARSDB).
- A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.
