Following the signal sequence from ribosomal tunnel exit to signal recognition particle

Mario Halic, Michael Blau, Thomas Becker, Thorsten Mielke, Martin R. Pool, Klemens Wild, Irmgard Sinning and Roland Beckmann ()
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Mario Halic: University of Munich
Michael Blau: University of Munich
Thomas Becker: University of Munich
Thorsten Mielke: UltraStructureNetwork, USN, Max Planck Institute for Molecular Genetics
Martin R. Pool: Michael Smith Building, University of Manchester
Klemens Wild: Heidelberg University Biochemistry Center (BZH)
Irmgard Sinning: Heidelberg University Biochemistry Center (BZH)
Roland Beckmann: University of Munich

Nature, 2006, vol. 444, issue 7118, 507-511

Abstract: Abstract Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane1. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome–nascent-chain complex to the protein-conducting channel at the membrane2,3. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome–SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.

Date: 2006
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DOI: 10.1038/nature05326

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