Recognition of a signal peptide by the signal recognition particle

Claudia Y. Janda, Jade Li, Chris Oubridge, Helena Hernández, Carol V. Robinson and Kiyoshi Nagai ()
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Claudia Y. Janda: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Jade Li: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Chris Oubridge: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Helena Hernández: University of Cambridge Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK
Carol V. Robinson: University of Cambridge Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK
Kiyoshi Nagai: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

Nature, 2010, vol. 465, issue 7297, 507-510

Abstract: Signal peptide binding to SRP545 The signal recognition particle (SRP) mediates targeting of nascent proteins to the plasma membrane in prokaryotes and the endoplasmic reticulum in eukaryotes. Secretory and membrane proteins contain a signal peptide at their N-termini, which is recognized by the SRP as it emerges from the ribosome. A universally conserved component of the SRP, known as SRP54, or its bacterial homologue Ffh, binds to the diverse range of signal peptides. In this study Janda et al. present the crystal structure of SRP54 and a signal peptide from Sulfolobus solfataricus, which reveals the mode of signal peptide recognition.

Date: 2010
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DOI: 10.1038/nature08870

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