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Analysis of the role of amino-terminal acetylation in modulating the cellular distribution and physical properties of the Parkinson's disease associated protein alpha-synuclein

Eastwood, Tara Ann (2016) Analysis of the role of amino-terminal acetylation in modulating the cellular distribution and physical properties of the Parkinson's disease associated protein alpha-synuclein. Master of Science by Research (MScRes) thesis, University of Kent,.

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Abstract

Alpha-Synuclein (aS) is a small, 140 amino acid, neuronal protein, found predominantly in the presynaptic terminals of neurons. Although the precise cellular function of ?S remains unknown, it is known to be critical in the pathology of a number of neurodegenerative disorders including Parkinson's Disease (PD) and other related dementias. A common symptomatic feature of PD and ?S associated disease states, is the aggregation of misfolded ?S into Lewy bodies. ?S is subject to a number of post-translational modifications, including amino-terminal (Nt) acetylation and is known to bind to membranes, both are believed to effect oligomer formation and the accumulation of ?S aggregates. In this project I am using different microbial model systems to examine the effect of Nt-acetylation on membrane binding and oligomer formation and their effect on the accumulation of ?S aggregates within the cell. The first model system used is the bacteria E. coli, in which we are making use of a novel Nt-acetylation system developed within this lab. The second model system being used is the fission yeast Schizosaccharomyces pombe, which allows us to use molecular genetic approaches to examine how the post-translational modification of Nt-acetylation effects ?S within a eukaryotic cell.

Item Type: Thesis (Master of Science by Research (MScRes))
Thesis advisor: Mulvihill, Daniel
Uncontrolled keywords: Alpha-Synuclein amino-terminal (Nt) acetylation
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Users 1 not found.
Date Deposited: 29 Sep 2016 11:00 UTC
Last Modified: 29 May 2019 17:54 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/57566 (The current URI for this page, for reference purposes)
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