Please use this identifier to cite or link to this item:
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.
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.
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 SizeFormat 
FYP (Dynn Sim, U1940111K).pdf
  Until 2024-04-26
6.98 MBAdobe PDFUnder embargo until Apr 26, 2024

Page view(s)

Updated on Jun 26, 2022

Google ScholarTM


Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.