Molecular Mechanism and Structure of Trigger Factor Bound to the Translating Ribosome

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2008 May 24

PMID 18497744

Citations 68

Authors

Frieder Merz

Daniel Boehringer

Christiane Schaffitzel

Steffen Preissler

Anja Hoffmann

Timm Maier

Anna Rutkowska

Jasmin Lozza

Nenad Ban

Bernd Bukau

Elke Deuerling

Affiliations

Soon will be listed here.

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.

Citing Articles

Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in .

Havermark T, Metelev M, Lundin E, Volkov I, Johansson M Proc Natl Acad Sci U S A. 2024; 122(1):e2409536121.

PMID: 39739798 PMC: 11725819. DOI: 10.1073/pnas.2409536121.

Bayesian reweighting of biomolecular structural ensembles using heterogeneous cryo-EM maps with the cryoENsemble method.

Wlodarski T, Streit J, Mitropoulou A, Cabrita L, Vendruscolo M, Christodoulou J Sci Rep. 2024; 14(1):18149.

PMID: 39103467 PMC: 11300795. DOI: 10.1038/s41598-024-68468-7.

Resolving chaperone-assisted protein folding on the ribosome at the peptide level.

Wales T, Pajak A, Roeselova A, Shivakumaraswamy S, Howell S, Kjaer S Nat Struct Mol Biol. 2024; 31(12):1888-1897.

PMID: 38987455 PMC: 11638072. DOI: 10.1038/s41594-024-01355-x.

Thermodynamic profiles for cotranslational trigger factor substrate recognition.

Herling T, Cassaignau A, Wentink A, Peter Q, Kumar P, Kartanas T Sci Adv. 2024; 10(28):eadn4824.

PMID: 38985872 PMC: 11235164. DOI: 10.1126/sciadv.adn4824.

Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.

Huang C, Lai Y, Chen S, Ho M, Chiang Y, Hsu S Magn Reson (Gott). 2023; 2(1):375-386.

PMID: 37904759 PMC: 10539794. DOI: 10.5194/mr-2-375-2021.

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