Journal
FEBS LETTERS
Volume 595, Issue 3, Pages 310-323Publisher
WILEY
DOI: 10.1002/1873-3468.14013
Keywords
amyotrophic lateral sclerosis; frontotemporal lobar degeneration; FUS; G‐ quadruplex (G4); RNA; TDP‐ 43
Funding
- Japan Society for the Promotion of Science (JSPS) [17K07291]
- Grants-in-Aid for Scientific Research [17K07291] Funding Source: KAKEN
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The study found that TDP-43 and FUS have different target selectivity in binding to G4-RNA, with TDP-43 recognizing parallel-stranded G4-DNA/RNAs and FUS binding to all three types of G4-DNA/RNAs.
Amyotrophic lateral sclerosis/frontotemporal lobar degeneration-linked proteins, TDP-43 and fused in sarcoma (FUS), bind to G-quadruplex-containing mRNAs and transport them to distal neurites for local translation. The specificity and mechanism of G4-RNA binding, however, remain largely unsolved. Using purified full-length TDP-43 and FUS and a set of seven G4-DNA/RNA, we compared their recognition properties of G4-RNAs. Both TDP-43 and FUS recognized and bound to G4-DNA/RNAs, but the target selectivity differed between two proteins. TDP-43 recognized only parallel-stranded G4-DNA/RNAs, leading to stabilize the G4 conformation. In contrast, FUS bound to all three types, parallel, hybrid, and antiparallel, of G4-DNA/RNAs, resulting in deformation of the G4 structure. We then concluded that the target selectivity and the influence on G4 RNA structure differed between TDP-43 and FUS.
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