Table 1 In vitro evidence for amyloid formation by RRMs and peptides within RRMs.
From: RNA recognition motifs of disease-linked RNA-binding proteins contribute to amyloid formation
RRM Domain/Peptide Residue numbers | ThT-binding fluorescence signal | Fibrils in EM or AFM | X-ray diffraction cross-β patterns | FTIR | Reference | |
|---|---|---|---|---|---|---|
TDP-43 RRM1 | 101–191 | Yes | Yes | Yes | Yes | This study |
TDP-43 RRM1 β2a peptide | 130–137 | No | Yes | Yes | Yes | |
TDP-43 RRM1 β2b peptide | 128–137 | No | Yes | Yes | Yes | |
FUS RRM | 281–375 | Yes | Yes | Yes | Yes | |
FUS RRM β2 peptide | 321–326 | No | Yes | Yes | Yes | |
TDP-43 RRM2peptide | 247–254 | Yes | Yes | Yes | NA | ref.31 |
TDP-43 RRM1 peptide | 128–135 | Not clear | Yes | No | NA | |
TDP-43 RRM2 peptides | 247–252, 247–255, 247–256, 247–257, 248–253, 248–256, 248–257, 251–259, 252–257 252–258, 253–258 | NA | Yes | Yes | NA | ref.32 |
TDP-43 RRM1 | 102–191 | Yes | Amorphous aggregates | NA | NA | ref.29 |
TDP-43 RRM1-2 | 102–269 | Yes | Amorphous aggregates | NA | NA | |
FUS RRM | 282–371 | Yes | Yes | NA | NA | ref.39 |
TDP-43 | ref.26 | |||||
Truncated RRM2 | 208–265 | Yes | Yes | NA | NA | |
TDP-43 RRM2 | ||||||
β3 peptides | 227–233 | No | Yes | NA | NA | |
β5 peptide | 253–259 | No | Yes | NA | NA | |
