Identification of molecular interactions between P-site tRNA and the ribosome essential for translocation
AUTOR(ES)
Feinberg, Jason S.
FONTE
The National Academy of Sciences
RESUMO
Translocation of the tRNA–mRNA complex is a fundamental step in the elongation cycle of protein synthesis. Our studies show that the ribosome can translocate a P-site-bound tRNAMet with a break in the phosphodiester backbone between positions 56 and 57 in the TΨC-loop. We have used this fragmented P-site-bound tRNAMet to identify two 2′-hydroxyl groups at positions 71 and 76 in the 3′-acceptor arm that are essential for translocation. Crystallographic data show that the 2′-hydroxyl group at positions 71 and 76 contacts the backbone of 23S rRNA residues 1892 and 2433–2434, respectively, in the ribosomal E site. These results establish a set of functional interactions between P-site tRNA and 23S rRNA that are essential for translocation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=58693Documentos Relacionados
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