PMID:11168582
| Citation |
Ishino, T, Atarashi, K, Uchiyama, S, Yamami, T, Saihara, Y, Yoshida, T, Hara, H, Yokose, K, Kobayashi, Y and Nakamura, Y (2000) Interaction of ribosome recycling factor and elongation factor EF-G with E. coli ribosomes studied by the surface plasmon resonance technique. Genes Cells 5:953-63 |
|---|---|
| Abstract |
Ribosome recycling factor (RRF), in concert with elongation factor EF-G, is required for disassembly of the post-termination complex of a ribosome after the release of polypeptides. How RRF dissociates the complex has long been puzzling. Crystal structures of RRF molecules have been solved recently and shown to mimic a transfer RNA (tRNA) shape, which prompted us to examine whether RRF binds to the ribosome as tRNA does. |
| Links | |
| Keywords |
Amino Acid Substitution/genetics; Aminoglycosides; Anti-Bacterial Agents/pharmacology; Arginine/genetics; Biological Transport, Active/drug effects; Biological Transport, Active/genetics; Escherichia coli/metabolism; Fusidic Acid/pharmacology; Glycine/genetics; Histidine/genetics; Mutagenesis, Site-Directed; Peptide Elongation Factor G/metabolism; Polyribosomes/drug effects; Polyribosomes/genetics; Polyribosomes/metabolism; Protein Binding/drug effects; Protein Binding/genetics; Protein Synthesis Inhibitors/pharmacology; Proteins/metabolism; RNA Stability/drug effects; RNA Stability/genetics; RNA, Ribosomal/metabolism; Ribosomal Proteins; Ribosomes/drug effects; Ribosomes/genetics; Ribosomes/metabolism; Surface Plasmon Resonance/methods; Thiostrepton/pharmacology |
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