Early encounters of a nascent membrane protein : specificity and timing of contacts inside and outside the ribosome

E.N.G. Houben, R. Zarivach, J Brunner, B. Oudega, S. Luirink

    Research output: Contribution to JournalArticleAcademicpeer-review

    86 Downloads (Pure)

    Abstract

    An unbiased photo-cross-linking approach was used to probe the "molecular path" of a growing nascent Escherichia coli inner membrane protein (IMP) from the peptidyl transferase center to the surface of the ribosome. The nascent chain was initially in proximity to the ribosomal proteins L4 and L22 and subsequently contacted L23, which is indicative of progression through the ribosome via the main ribosomal tunnel. The signal recognition particle (SRP) started to interact with the nascent IMP and to target the ribosome-nascent chain complex to the Sec-YidC complex in the inner membrane when maximally half of the transmembrane domain (TM) was exposed from the ribosomal exit. The combined data suggest a flexible tunnel that may accommodate partially folded nascent proteins and parts of the SRP and SecY. Intraribosomal contacts of the nascent chain were not influenced by the presence of a functional TM in the ribosome. © The Rockefeller University Press.
    Original languageEnglish
    Pages (from-to)27-35
    Number of pages9
    JournalJournal of Cell Biology
    Volume170
    DOIs
    Publication statusPublished - 2005

    Fingerprint

    Dive into the research topics of 'Early encounters of a nascent membrane protein : specificity and timing of contacts inside and outside the ribosome'. Together they form a unique fingerprint.

    Cite this