[Ribosome recycling revisited].
Ribosome recycling involves the coordinated action of the ribosome recycling factor (RRF), elongation factor EF-G and initiation factor IF3 to disassemble the post-termination complex, recycling the components for the next round of translation. The crystal structure of domain I of RRF (RRF-DI) in complex with the large ribosomal subunit from the eubacteria Deinococcus radiodurans at high resolution reveals the nature and details of the interactions between this protein factor and rRNA/protein components of the ribosome. Universally conserved arginine residues within the RRF-DI establish important interactions with nuleotides of the 23S rRNA, explaining why mutations at these positions abolish factor binding. Furthermore, in conjunction with cryo-EM reconstruction, the X-ray analysis provides a structural complement to the recent biochemical data, offering additional insight into the mechanism of ribosome recycling.
Vesper
Oliver
O
Wilson
Daniel N
DN
D001120:Arginine / Q000378:metabolism; D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D034301:Deinococcus / Q000378:metabolism; D039621:Eukaryotic Initiation Factor-3 / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D020653:Peptide Elongation Factor G / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D014176:Protein Biosynthesis / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000502:physiology*
D001426:Bacterial Proteins; D039621:Eukaryotic Initiation Factor-3; D020653:Peptide Elongation Factor G; D012269:Ribosomal Proteins; C087267:ribosome releasing factor; D001120:Arginine