How a Toxin's C-Terminal Peptide Helps It Fold and Function
Author Information
Author(s): Iacovache Ioan, Degiacomi Matteo T., Pernot Lucile, Ho Sylvia, Schiltz Marc, Dal Peraro Matteo, van der Goot F. Gisou
Primary Institution: Ecole Polytechnique Fédérale de Lausanne, Switzerland
Hypothesis
What role does the C-terminal propeptide play in the folding and oligomerization of the pore-forming toxin aerolysin?
Conclusion
The C-terminal propeptide is essential for the proper folding of aerolysin into a soluble form and prevents premature aggregation.
Supporting Evidence
- The C-terminal propeptide prevents aggregation during the folding of aerolysin.
- Mutations in the C-terminal propeptide lead to improper folding and aggregation of the toxin.
- The C-terminal propeptide acts as a dual-function chaperone, aiding both folding and assembly.
- Addition of synthetic CTP can partially restore activity in aerolysin lacking its propeptide.
Takeaway
Aerolysin, a toxin produced by bacteria, needs a special piece at its end to fold correctly and not clump together before it can work.
Methodology
The study combined computational techniques with experimental validation using structural and functional approaches to investigate the role of the C-terminal propeptide in aerolysin folding.
Statistical Information
P-Value
p<0.005
Statistical Significance
p<0.005
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website