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Recognition of a signal peptide by the signal recognition particle

Author

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  • Claudia Y. Janda

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
    Present addresses: Department of Molecular and Cellular Physiology and Department of Structural Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA (C.Y.J.); Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK (H.H. and C.V.R.).)

  • 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
    Present addresses: Department of Molecular and Cellular Physiology and Department of Structural Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA (C.Y.J.); Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK (H.H. and C.V.R.).)

  • Carol V. Robinson

    (University of Cambridge Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, UK
    Present addresses: Department of Molecular and Cellular Physiology and Department of Structural Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA (C.Y.J.); Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK (H.H. and C.V.R.).)

  • Kiyoshi Nagai

    (MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK)

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.

Suggested Citation

  • Claudia Y. Janda & Jade Li & Chris Oubridge & Helena Hernández & Carol V. Robinson & Kiyoshi Nagai, 2010. "Recognition of a signal peptide by the signal recognition particle," Nature, Nature, vol. 465(7297), pages 507-510, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7297:d:10.1038_nature08870
    DOI: 10.1038/nature08870
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