PMID:15228531
| Citation |
Fujiwara, T, Ito, K, Yamami, T and Nakamura, Y (2004) Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor G. Mol. Microbiol. 53:517-28 |
|---|---|
| Abstract |
Ribosome recycling factor (RRF) disassembles post-termination ribosomal complexes in concert with elongation factor EF-G freeing the ribosome for a new round of polypeptide synthesis. How RRF interacts with EF-G and disassembles post-termination ribosomes is unknown. RRF is structurally similar to tRNA and is therefore thought to bind to the ribosomal A site and be translocated by EF-G during ribosome disassembly as a mimic of tRNA. However, EF-G variants that remain active in GTP hydrolysis but are defective in tRNA translocation fully activate RRF function in vivo and in vitro. Furthermore, RRF and the GTP form of EF-G do not co-occupy the terminating ribosome in vitro; RRF is ejected by EF-G from the preformed complex. These findings suggest that RRF is not a functional mimic of tRNA and disassembles the post-termination ribosomal complex independently of the translocation activity of EF-G. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2004.04156.x |
| Keywords |
Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Genes, Bacterial; Genes, Essential; Guanosine Triphosphate/metabolism; Models, Molecular; Mutation; Peptide Elongation Factor G/genetics; Peptide Elongation Factor G/physiology; Protein Binding; Protein Biosynthesis; Proteins/genetics; Proteins/physiology; RNA, Transfer/metabolism; Ribosomal Proteins; Ribosomes/metabolism; Ribosomes/physiology |
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