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Examining prionogenic domains in the Swi1 protein, yeast evolution, and novel disease-related aggregators

Description:

Prions are self-perpetuating, alternative protein conformations associated with neurological diseases and normal cellular functions. Saccharomyces cerevisiae contains many endogenous prions – providing a powerful system to study prionization. Previously, the Li Lab demonstrated that Swi1, a component of the SWI/SNF chromatin-remodeling complex, can form the prion [SWI+]. A small region,...

Keyword:

[SWI+], yeast, protein aggregation, prions, Saccharomyces cerevisiae, and Swi1

Subject:

Molecular biology, Bioinformatics, and Neurosciences

Creator:

Goncharoff, Dustin Kenneth

Owner:

Scholarly Digital Publishing

Language:

en

Date Uploaded:

06/28/2021

Date Created:

2021-01-01

Resource Type:

Dissertation

Alternate Identifier:

etdadmin_upload_816388 and http://dissertations.umi.com/northwestern:15538
Using the [SWI+] prion to study protein misfolding, aggregation, and amyloid formation

Description:

Saccharomyces cerevisiae contains several epigenetic elements known as yeast prions. Our laboratory discovered the yeast prion [SWI+], whose protein determinant is Swi1, a subunit of the SWI/SNF chromatin-remodeling complex. Formation of [SWI+] results in abolishment of multicellular features and a partial loss-of-function phenotype of non-glucose carbon source usage. Our laboratory...

Keyword:

amyloids, protein aggregation, prion, Saccharomyces cerevisiae, Swi1, and prion domain

Subject:

Interdepartmental Neuroscience Program (NUIN)

Creator:

Stephanie Valtierra

Owner:

Scholarly Digital Publishing

Date Uploaded:

10/26/2018

Date Modified:

10/26/2018

Date Created:

2017-01-01

Resource Type:

Dissertation

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Examining prionogenic domains in the Swi1 protein, yeast evolution, and novel disease-related aggregators

Using the [SWI+] prion to study protein misfolding, aggregation, and amyloid formation

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