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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||Fulltext Permission:||embargo_restricted_20240426||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Student Reports (FYP/IA/PA/PI)|
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|FYP (Dynn Sim, U1940111K).pdf|
|6.98 MB||Adobe PDF||Under embargo until Apr 26, 2024|
Updated on May 26, 2022
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