Article
- The EMBO Journal (2005) 24, 251 - 260
- doi:10.1038/sj.emboj.7600525
Published online: 23 December 2004
Subject Categories:
X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit
Daniel N Wilson1,4, Frank Schluenzen1,4, Joerg M Harms2,4, Takuya Yoshida3, Tadayasu Ohkubo3, Renate Albrecht1, Joerg Buerger1, Yuji Kobayashi3 and Paola Fucini1
- Max-Planck-Institute for Molecular Genetics, Berlin, Germany
- Riboworld.com, Hamburg, Germany
- Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan
- These authors contributed equally to this work
Correspondence to:
Frank Schluenzen, Max-Planck-Institute for Molecular Genetics, Ihnestr. 73, Berlin 14195, Germany. Tel.: +49 (0) 40 8998 2809; Fax: +49 (0) 40 8971 6848; E-mail: schluenz@molgen.mpg.de
Paola Fucini, Max-Planck-Institute for Molecular Genetics, Ihnestr. 73, Berlin 14195, Germany. Tel.: +49 (0) 30 8413 1691; Fax: +49 (0) 30 8413 1690; E-mail: fucini@molgen.mpg.de
Received 23 September 2004; Accepted 26 November 2004
Abstract
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 
-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.
Keywords:
- crystallography,
- elongation factor G,
- protein synthesis,
- ribosome recycling,
- ribosome recycling factor
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