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X‐ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit
Author(s) -
Wilson Daniel N,
Schluenzen Frank,
Harms Joerg M,
Yoshida Takuya,
Ohkubo Tadayasu,
Albrecht Renate,
Buerger Joerg,
Kobayashi Yuji,
Fucini Paola
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600525
Subject(s) - biology , ribosome , protein subunit , ribosomal rna , 50s , ribosomal protein , mechanism of action , mechanism (biology) , biochemistry , rna , gene , physics , in vitro , quantum mechanics
This study presents the crystal structure of domain I of the Escherichia coli ribosome recycling factor (RRF) bound to the Deinococcus radiodurans 50S subunit. The orientation of RRF is consistent with the position determined on a 70S‐RRF complex by cryoelectron microscopy (cryo‐EM). Alignment, however, requires a rotation of 7° and a shift of the cryo‐EM RRF by a complete turn of an α‐helix, redefining the contacts established with ribosomal components. At 3.3 Å resolution, RRF is seen to interact exclusively with ribosomal elements associated with tRNA binding and/or translocation. Furthermore, these results now provide a high‐resolution structural description of the conformational changes that were suspected to occur on the 70S‐RRF complex, which has implications for the synergistic action of RRF with elongation factor G (EF‐G). Specifically, the tip of the universal bridge element H69 is shifted by 20 Å toward h44 of the 30S subunit, suggesting that RRF primes the intersubunit bridge B2a for the action of EF‐G. Collectively, our data enable a model to be proposed for the dual action of EF‐G and RRF during ribosome recycling.