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Science 5 May 2006:
Vol. 312. no. 5774, pp. 745 - 747
DOI: 10.1126/science.1124864
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Reports

Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site

Mario Halic,1* Marco Gartmann,1* Oliver Schlenker,2 Thorsten Mielke,3 Martin R. Pool,4 Irmgard Sinning,2 Roland Beckmann1,3*{dagger}

Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo–electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain–mediated elongation arrest persisted.

1 Institute of Biochemistry, Charité, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany.
2 Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
3 UltraStructureNetwork, USN, Max Planck Institute for Molecular Genetics, Ihnestrasse 63-73, 14195 Berlin, Germany.
4 University of Manchester, Faculty of Life Sciences, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.

* Present address: Gene Center, University of Munich, Department of Chemistry and Biochemistry, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.

{dagger} To whom correspondence should be addressed. E-mail: beckmann{at}lmb.uni-muenchen.de

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