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Molecular basis of [PSI+] yeast prion nucleation

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dc.contributor.authorBen Musa, Zobaida A., author
dc.contributor.authorRoss, Eric, advisor
dc.contributor.authorCrans, Debbie, committee member
dc.contributor.authorZabel, Mark, committee member
dc.contributor.authorDi Pietro, Santiago, committee member
dc.date.accessioned2007-01-03T06:08:42Z
dc.date.available2007-01-03T06:08:42Z
dc.date.issued2013
dc.description.abstractMany fatal diseases arise from the conversion of soluble, functional proteins to insoluble misfolded amyloid aggregates. Amyloid fibers are characterized by filamentous morphology, protease resistance and cross]beta structure. Prions (infectious amyloids) are a specific subset of amyloid fibers, differing from other classes of amyloids by their infectivity. Prions are found in both mammals and yeasts, but there are differences between these two groups. Most yeast prions are characterized by the presence of large numbers of glutamine and asparagine (Q/N) residues, and some other common characteristics have been noted, including the presence of few hydrophobic and charged residues. Although, several attempts have been made with limited success to develop valuable systems to predict prion activity, there is no accurate algorithm that has the ability to predict the prion-forming proteins among the Q/N-rich protein group. In the yeast, it has been shown that amino acid composition, not primary sequence, drives prion activity. Recently, preliminary efforts to define the role of amino acid composition in prion formation have been examined. The fundamental question of this project is how, in yeast Q/N-rich prions, the sequence requirements for nucleation versus propagation differ, and how this information can be used in order to develop a precise prion prediction system. By answering this question we will be able to more accurately identify additional prions in both yeast and other organisms. Our long-term goal in the comprehensive studies of prion formation and propagation mechanisms is to apply this information to mammalian prion diseases. Consequently, we will be able to identify targets for therapeutic intervention to avoid, slow-down, or reverse the development of related diseases. The study determined that the amino acids required for prion formation differ from those required for prion propagation. Identifying the sequence feature for both activities is the first step towards mechanistic studies to examine how these sequences perform their function.
dc.format.mediumborn digital
dc.format.mediumdoctoral dissertations
dc.identifierbenmusa_colostate_0053A_12119.pdf
dc.identifierETDF2013500289CMBO
dc.identifier.urihttp://hdl.handle.net/10217/80933
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.subjectprion
dc.subjectsup35
dc.titleMolecular basis of [PSI+] yeast prion nucleation
dc.typeText
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineCell and Molecular Biology
thesis.degree.grantorColorado State University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy (Ph.D.)

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