Identification of nascent chain interaction sites on trigger factor

Sathish K. Lakshmipathy, Sladjana Tomic, Christian M. Kaiser, Hung Chun Chang, Pierre Genevaux, Costa Georgopoulos, José M. Barral, Arthur E. Johnson, F. Ulrich Hartl, Stephanie A. Etchells

    Research output: Contribution to journalArticle

    55 Scopus citations

    Abstract

    The role of ribosome-binding molecular chaperones in protein folding is not yet well understood. Trigger factor (TF) is the first chaperone to interact with nascent polypeptides as they emerge from the bacterial ribosome. It binds to the ribosome as a monomer but forms dimers in free solution. Based on recent crystal structures, TF has an elongated shape, with the peptidylprolyl-cis/ trans-isomerase (PPIase) domain and the N-terminal ribosome binding domain positioned at opposite ends of the molecule and the C-terminal domain, which forms two arms, positioned in between. By using site specifically labeled TF proteins, we have demonstrated that all three domains of TF interact with nascent chains during translation. Interactions with the PPIase domain were length-dependent but independent of PPIase activity. Interestingly, with free TF, these same sites were found to be involved in forming the dimer interface, suggesting that dimerization partially occludes TF-nascent chain binding sites. Our data indicate the existence of two regions on TF along which nascent chains can interact, the NC-domains as the main site and the PPIase domain as an auxiliary site.

    Original languageEnglish (US)
    Pages (from-to)12186-12193
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume282
    Issue number16
    DOIs
    StatePublished - Apr 20 2007

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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    Lakshmipathy, S. K., Tomic, S., Kaiser, C. M., Chang, H. C., Genevaux, P., Georgopoulos, C., Barral, J. M., Johnson, A. E., Hartl, F. U., & Etchells, S. A. (2007). Identification of nascent chain interaction sites on trigger factor. Journal of Biological Chemistry, 282(16), 12186-12193. https://doi.org/10.1074/jbc.M609871200