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Chaperone and antichaperone activities of trigger factor.
Guo-Chang Huang1, Jia-Jia Chen, Chuan-Peng Liu
1National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
European Journal of Biochemistry
|September 17, 2002
Summary
Trigger factor, a protein folding catalyst, exhibits dual activity influencing lysozyme refolding. It can enhance protein recovery by acting as a chaperone or hinder it via antichaperone activity, impacting aggregation.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Folding
Background:
- Denatured lysozyme aggregation at neutral pH reduces refolding efficiency.
- Protein aggregation is a significant challenge in protein biosynthesis and refolding.
Purpose of the Study:
- To investigate the dual role of trigger factor in lysozyme refolding.
- To understand how trigger factor concentration and solution conditions modulate its chaperone or antichaperone activity.
Main Methods:
- Studied lysozyme refolding under varying trigger factor concentrations.
- Analyzed protein aggregation and reactivation rates.
- Investigated trigger factor's presence in aggregates using urea solubilization.
Main Results:
- Trigger factor demonstrated both chaperone (increased recovery, decreased aggregation) and antichaperone (decreased recovery, increased aggregation) activities.
- Chaperone activity correlated with decelerated refolding and reduced aggregation at higher trigger factor concentrations.
- Antichaperone activity correlated with accelerated refolding and increased aggregation.
- Trigger factor was found to be incorporated into lysozyme aggregates.
Conclusions:
- The dual effect of trigger factor on lysozyme refolding is concentration-dependent and linked to its peptide-binding ability.
- Trigger factor's activity may play a regulatory role in protein biosynthesis.
- Understanding trigger factor's function is crucial for controlling protein aggregation and refolding.