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Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing.

Authors
Type
Published Article
Journal
Cell
Publisher
Elsevier
Volume
111
Issue
1
Pages
129–140
Source
UCSC Bioinformatics biomedical-ucsc
License
Unknown

Abstract

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.

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