ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.

Abstract excerpt

TAR-DNA-binding protein-43 (TDP-43) C-terminus encodes a prion-like domain widely presented in RNA-binding proteins, which functions to form dynamic oligomers and also, amazingly, hosts most amyotrophic lateral sclerosis (ALS)-causing mutations. Here, as facilitated by our previous discovery, by circular dichroism (CD), fluorescence and nuclear magnetic resonance (NMR) spectroscopy, we have successfully...

Topics

• Amyotrophic Lateral Sclerosis
• Circular Dichroism
• DNA-Binding Proteins
• Humans
• Hydrogen-Ion Concentration
• Microscopy, Electron
• Molecular Probe Techniques
• Mutation
• Nucleic Acids
• Protein Structure, Tertiary