Initiation Factor 2-Dependent Ribosomal Binding of N-Formylmethionyl-Transfer RNA Without Added Guanosine Triphosphate
AUTOR(ES)
Mazumder, Rajarshi
RESUMO
Evidence is presented that suggests that GTP (or 5′-guanylylmethylene diphosphonate) is not essential for either formation of an AUG-directed, initiation factor IF-2-dependent initiation complex on the 30S subunit or for positioning of fMet-tRNA on the peptidyl site. However, recycling of limiting amounts of IF-2 requires both GTP and the 50S subunit. The formation of the complex IF-2-30S as an intermediate in polypeptidechain initiation is suggested.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389641Documentos Relacionados
- The role of guanosine 5'-triphosphate in the initiation of peptide synthesis. 3. Binding of formylmethionyl-tRNA to ribosomes.
- Factor- and guanosine 5'-triphosphate-dependent release of deacylated transfer RNA from 70S ribosomes.
- The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis
- ROLE OF GUANOSINE 5′-TRIPHOSPHATE IN THE INITIATION OF PEPTIDE SYNTHESIS, I. SYNTHESIS OF FORMYLMETHIONYL-PUROMYCIN*
- Protein Initiation in Eukaryotes: Formation and Function of a Ternary Complex Composed of a Partially Purified Ribosomal Factor, Methionyl Transfer RNAf, and Guanosine Triphosphate