Article
- The EMBO Journal (2008) 27, 1622 - 1632
- doi:10.1038/emboj.2008.89
Published online: 22 May 2008
Subject Category:
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
Frieder Merz1,a, Daniel Boehringer2,a, Christiane Schaffitzel2,b, Steffen Preissler1, Anja Hoffmann1, Timm Maier2, Anna Rutkowska1, Jasmin Lozza2, Nenad Ban2, Bernd Bukau1 and Elke Deuerling1,3
- Zentrum für Molekulare Biologie Heidelberg (ZMBH), DKFZ-ZMBH Alliance, Universität Heidelberg, Heidelberg, Germany
- Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
- Present address: Molekulare Mikrobiologie, Universität Konstanz, 78457 Konstanz, Germany
Correspondence to:
Bernd Bukau, Molekulare Mikrobiologie, University of Konstanz, Box M607, 78457 Konstanz, Germany. Tel.: +49 7531 882647; Fax: +49 7531 884036; E-mail: Bukau@zmbh.uni-heidelberg.de
Elke Deuerling, Molekulare Mikrobiologie, University of Konstanz, Box M607, 78457 Konstanz, Germany. Tel.: +49 7531 882647; Fax: +49 7531 884036; E-mail: elke.deuerling@uni-konstanz.de
aThese authors contributed equally to this work
bPresent address: EMBL Grenoble, 38042 Grenoble Cedex 9, France
Received 18 December 2007; Accepted 10 April 2008
Abstract
Ribosome-associated chaperone Trigger Factor (TF) initiates folding of newly synthesized proteins in bacteria. Here, we pinpoint by site-specific crosslinking the sequence of molecular interactions of Escherichia coli TF and nascent chains during translation. Furthermore, we provide the first full-length structure of TF associated with ribosome–nascent chain complexes by using cryo-electron microscopy. In its active state, TF arches over the ribosomal exit tunnel accepting nascent chains in a protective void. The growing nascent chain initially follows a predefined path through the entire interior of TF in an unfolded conformation, and even after folding into a domain it remains accommodated inside the protective cavity of ribosome-bound TF. The adaptability to accept nascent chains of different length and folding states may explain how TF is able to assist co-translational folding of all kinds of nascent polypeptides during ongoing synthesis. Moreover, we suggest a model of how TF's chaperoning function can be coordinated with the co-translational processing and membrane targeting of nascent polypeptides by other ribosome-associated factors.
Keywords:
- chaperone,
- nascent chains,
- protein folding,
- ribosome,
- Trigger Factor
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