Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site-Reference-Cited by-同舟云学术

Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site

Published:2006-05-05 Issue:5774 Volume:312 Page:745-747
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Halic Mario¹²³⁴,Gartmann Marco¹²³⁴,Schlenker Oliver¹²³⁴,Mielke Thorsten¹²³⁴,Pool Martin R.¹²³⁴,Sinning Irmgard¹²³⁴,Beckmann Roland¹²³⁴

Affiliation:

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.

Abstract

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 80 S 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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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