Logo Logo
Hilfe
Kontakt
Switch language to English
Real time observation of TF function on translating ribosomes
Real time observation of TF function on translating ribosomes
Ribosome-associated Trigger factor (TF) is the first molecular chaperone to bind to nascent polypeptides in bacteria. The contribution of co-translational chaperone function is yet poorly understood. Using fluorescence spectroscopy to monitor, in real time, TF function and structural rearrangements, the present study investigates how TF interacts with ribosomes and translating polypeptides. Binding to the ribosome stabilizes an open, activated conformation of TF. Conformationally activated TF can stay associated with its nascent polypeptide substrate beyond ribosome departure. The occurence of hydrophobic motifs in the translating polypeptide correlates with the duration of TF-substrate interaction, leading to prolonged interaction with a high aggregation propensity. These findings can explain the contribution of TF in preventing protein misfolding and reveal an exquisitely regulated interaction cycle of TF with ribosome-nascent chain complexes.
Protein Folding, Chaperone, Nascent Chain, Ribosome, Translation
Kaiser, Christian
2006
Englisch
Universitätsbibliothek der Ludwig-Maximilians-Universität München
Kaiser, Christian (2006): Real time observation of TF function on translating ribosomes. Dissertation, LMU München: Fakultät für Chemie und Pharmazie
[thumbnail of Kaiser_Christian.pdf]
Vorschau
PDF
Kaiser_Christian.pdf

7MB

Abstract

Ribosome-associated Trigger factor (TF) is the first molecular chaperone to bind to nascent polypeptides in bacteria. The contribution of co-translational chaperone function is yet poorly understood. Using fluorescence spectroscopy to monitor, in real time, TF function and structural rearrangements, the present study investigates how TF interacts with ribosomes and translating polypeptides. Binding to the ribosome stabilizes an open, activated conformation of TF. Conformationally activated TF can stay associated with its nascent polypeptide substrate beyond ribosome departure. The occurence of hydrophobic motifs in the translating polypeptide correlates with the duration of TF-substrate interaction, leading to prolonged interaction with a high aggregation propensity. These findings can explain the contribution of TF in preventing protein misfolding and reveal an exquisitely regulated interaction cycle of TF with ribosome-nascent chain complexes.