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  Signal recognition particle receptor exposes the ribosomal translocon binding site

Halic, M., Gartmann, M., Schlenker, O., Mielke, T., Pool, M. R., Sinning, I., et al. (2006). Signal recognition particle receptor exposes the ribosomal translocon binding site. Science, 312(5774), 745-747. doi:10.1126/science.1124864.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-842E-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-842F-7
Genre: Journal Article

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745.pdf (Any fulltext), 376KB
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 Creators:
Halic, Mario, Author
Gartmann, Marco, Author
Schlenker, Oliver, Author
Mielke, Thorsten1, Author              
Pool, Martin R., Author
Sinning, Irmgard, Author
Beckmann, Roland2, Author
Affiliations:
1Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
2Max Planck Society, ou_persistent13              

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 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 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.

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Language(s): eng - English
 Dates: 2006-05-05
 Publication Status: Published in print
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 Identifiers: eDoc: 307710
DOI: 10.1126/science.1124864
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 312 (5774) Sequence Number: - Start / End Page: 745 - 747 Identifier: ISSN: 0036-8075