Real-time observation of trigger factor function on translating ribosomes

Christian M. Kaiser, Hung-Chun Chang, Vishwas R. Agashe, Sathish K. Lakshmipathy, Stephanie A. Etchells, Manajit Hayer-Hartl, F. Ulrich Hartl and José M. Barral ()
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Christian M. Kaiser: Max Planck Institute of Biochemistry
Hung-Chun Chang: Max Planck Institute of Biochemistry
Vishwas R. Agashe: Max Planck Institute of Biochemistry
Sathish K. Lakshmipathy: Max Planck Institute of Biochemistry
Stephanie A. Etchells: Max Planck Institute of Biochemistry
Manajit Hayer-Hartl: Max Planck Institute of Biochemistry
F. Ulrich Hartl: Max Planck Institute of Biochemistry
José M. Barral: Max Planck Institute of Biochemistry

Nature, 2006, vol. 444, issue 7118, 455-460

Abstract: Abstract The contribution of co-translational chaperone functions to protein folding is poorly understood. Ribosome-associated trigger factor (TF) is the first molecular chaperone encountered by nascent polypeptides in bacteria. Here we show, using fluorescence spectroscopy to monitor TF function and structural rearrangements in real time, that TF interacts with ribosomes and translating polypeptides in a dynamic reaction cycle. Ribosome binding stabilizes TF in an open, activated conformation. Activated TF departs from the ribosome after a mean residence time of ∼10 s, but may remain associated with the elongating nascent chain for up to 35 s, allowing entry of a new TF molecule at the ribosome docking site. The duration of nascent-chain interaction correlates with the occurrence of hydrophobic motifs in translating polypeptides, reflecting a high aggregation propensity. These findings can explain how TF prevents misfolding events during translation and may provide a paradigm for the regulation of nucleotide-independent chaperones.

Date: 2006
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DOI: 10.1038/nature05225

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