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Title: | Roles of TDP-43 domains in RNA-free phase separation | Authors: | Sim, Dynn | Keywords: | Science::Biological sciences::Molecular biology | Issue Date: | 2022 | Publisher: | Nanyang Technological University | Source: | Sim, D. (2022). Roles of TDP-43 domains in RNA-free phase separation. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/156887 | Abstract: | TAR-DNA-binding protein (TDP-43) has remained the central focus of research into Amyotrophic Lateral Sclerosis (ALS) since its discovery as the primary component of pathological inclusions in ALS patients. RNA-deficient TDP-43 was shown to demix into spherical shell-like condensates, which was suggested to be the precursor of the cytoplasmic aggregates. In this study, I investigated how each TDP-43 domain contributes to the formation of TDP-43 spherical shells. In particular, the role of the RNA recognition motifs (RRMs) during the shell-like phase separation was thoroughly examined. Self-association of TDP-43 via NTD (N-terminal domain) appeared to be crucial for the aggregation or phase separation of wild-type and RNA-binding deficient TDP-43. Notably, neither the NTD nor the LCD (low complexity domain) could phase separate when they were separate from each other. I also examined if the NTD and the LCD are transferrable to other proteins. This study will give insights into the condensation and aggregation mechanism of pathologic TDP-43. | URI: | https://hdl.handle.net/10356/156887 | Schools: | School of Biological Sciences | Fulltext Permission: | embargo_restricted_20240426 | Fulltext Availability: | With Fulltext |
Appears in Collections: | SBS Student Reports (FYP/IA/PA/PI) |
Files in This Item:
File | Description | Size | Format | |
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FYP (Dynn Sim, U1940111K).pdf Until 2024-04-26 | 6.98 MB | Adobe PDF | Under embargo until Apr 26, 2024 |
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