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Originally published In Press as doi:10.1074/jbc.M206295200 on July 22, 2002

J. Biol. Chem., Vol. 277, Issue 39, 35847-35852, September 27, 2002
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Binding of Ribosome Recycling Factor to Ribosomes, Comparison with tRNA*

Go HirokawaDagger §, Michael C. KielDagger , Aiko MutoDagger , Gota Kawai||, Kazuei Igarashi§, Hideko Kaji**, and Akira KajiDagger Dagger Dagger

From the Dagger  Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, the § Department of Clinical Biochemistry, Graduate School of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, the || Department of Industrial Chemistry, Chiba Institute of Technology, 2-17-1 Tsudanuma, Narashino-shi, Chiba 275-8588, Japan, and the ** Department of Biochemistry and Molecular Pharmacology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

The prokaryotic post-termination ribosomal complex is disassembled by ribosome recycling factor (RRF) and elongation factor G. Because of the structural similarity of RRF and tRNA, we compared the biochemical characteristics of RRF binding to ribosomes with that of tRNA. Unesterified tRNA inhibited the disassembly of the post-termination complex in a competitive manner with RRF, suggesting that RRF binds to the A-site. Approximately one molecule of ribosome-bound RRF was detected after isolation of the RRF-ribosome complex. RRF and unesterified tRNA similarly inhibited the binding of N-acetylphenylalanyl-tRNA to the P-site of non-programmed but not programmed ribosomes. Under the conditions in which unesterified tRNA binds to both the P- and E-sites of non-programmed ribosomes, RRF inhibited 50% of the tRNA binding, suggesting that RRF does not bind to the E-site. The results are consistent with the notion that a single RRF binds to the A- and P-sites in a somewhat analogous manner to the A/P-site bound peptidyl tRNA. The binding of RRF and tRNA to ribosomes was influenced by Mg2+ and NH<UP><SUB>4</SUB><SUP>+</SUP></UP> ions in a similar manner.

* This work was supported in part by National Institutes of Health Grant 1-R01-GH-60429-01A2 (to A. K.) and Nippon Paint Research Fund (to H. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by Japan Society for the Promotion of Science Research Fellowships for Young Scientists.

Dagger Dagger To whom correspondence should be addressed: Dept. of Microbiology, University of Pennsylvania School of Medicine, Room 203B, Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104. Tel.: 215-898-8828; Fax: 215-573-2221; E-mail: kaji@mail.med.upenn.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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