Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/148412
Title: Characterization of ALS-associated proteins in Saccharomyces cerevisiae
Authors: Ng, Qing Hao
Keywords: Science::Biological sciences
Issue Date: 2021
Publisher: Nanyang Technological University
Source: Ng, Q. H. (2021). Characterization of ALS-associated proteins in Saccharomyces cerevisiae. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/148412
Abstract: Various mutations in the low complexity domain of RNA-binding proteins such as TDP-43, FUS and hnRNPA1 have been identified from familial ALS (Amyotrophic Lateral Sclerosis) patients. Aggregation of these RNA-binding proteins, particularly TDP-43, is a hallmark of ALS. It is notable that these ALS-associated RNA-binding proteins can be sequestered in stress granules that form transiently during stress conditions. During aging, however, stress granules become chronic and thus, the retention time of RNA-binding proteins in stress granules becomes prolonged. Furthermore, the high local concentration of RNA-binding proteins can lead to their aggregation. In this project, I show that RNA-binding proteins can also be sequestered to processing bodies, another type of cytosolic ribonucleoprotein granule. I next asked if sequestration of TDP-43 in stress granules or processing bodies depends on its RNA-binding property. Surprisingly, mutations in RNA recognition motifs of TDP-43 resulted in the formation of perinuclear annular structures that did not colocalize with cytosolic ribonucleoprotein granules. Investigation of this unique structure is expected to shed light on the mechanism of TDP-43 aggregation.
URI: https://hdl.handle.net/10356/148412
Fulltext Permission: embargo_restricted_20230427
Fulltext Availability: With Fulltext
Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)

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