Orientation of Ribosome Recycling Factor in the Ribosome from Directed Hydroxyl Radical Probing
Autor: | Harry F. Noller, Laura Lancaster, Michael C. Kiel, Akira Kaji |
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Rok vydání: | 2002 |
Předmět: |
Models
Molecular Ribosomal Proteins Ribosome Recycling Factor Ribosome General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Protein structure RNA Transfer Ribosomal protein RNA Ribosomal 16S Escherichia coli 030304 developmental biology 0303 health sciences biology Hydroxyl Radical Biochemistry Genetics and Molecular Biology(all) 030302 biochemistry & molecular biology Proteins Translation (biology) Protein Structure Tertiary Elongation factor RNA Ribosomal 23S Biochemistry Mutation Transfer RNA Mutagenesis Site-Directed biology.protein Biophysics Nucleic Acid Conformation T arm Ribosomes Plasmids Protein Binding |
Zdroj: | Cell. 111(1):129-140 |
ISSN: | 0092-8674 |
DOI: | 10.1016/s0092-8674(02)00938-8 |
Popis: | Ribosome recycling factor (RRF) disassembles posttermination complexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of translation. The striking resemblance of its L-shaped structure to that of tRNA has suggested that the mode of action of RRF may be based on mimicry of tRNA. Directed hydroxyl radical probing of 16S and 23S rRNA from Fe(II) tethered to ten positions on the surface of E. coli RRF constrains it to a well-defined location in the subunit interface cavity. Surprisingly, the orientation of RRF in the ribosome differs markedly from any of those previously observed for tRNA, suggesting that structural mimicry does not necessarily reflect functional mimicry. |
Databáze: | OpenAIRE |
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