Involvement of a specific ubiquitin ligase in the assembly of the dynein motor in the filamentous fungus Neurospora crassa

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Involvement of a specific ubiquitin ligase in the assembly of the dynein motor in the filamentous fungus Neurospora crassa

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/14953

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dc.contributor.author Elsenpeter, Ryan Lee
dc.date.accessioned 2012-08-27T17:36:25Z
dc.date.available 2012-08-27T17:36:25Z
dc.date.issued 2012-08-27
dc.date.submitted 2012 Summer en
dc.identifier.uri http://hdl.handle.net/10355/14953
dc.description Title from PDF of title page, viewed on August 27, 2012 en
dc.description Dissertation advisor: Michael Plamann en
dc.description Vita en
dc.description Includes bibliographic references (p. 130-143) en
dc.description Thesis (Ph.D.)--School of Biological Sciences. University of Missouri--Kansas City, 2012 en
dc.description.abstract Eukaryotic cells utilize multiple molecular motor proteins to accomplish intracellular transport. The two microtubule based motors, kinesin and cytoplasmic dynein, work in concert to move cargoes outward and inward, respectively, in the cell. In polarized cells, molecular motors are of even greater importance due to a need for long distance transport and maintenance of proper polarity. Although there exists numerous forms of kinesin for anterograde transport, only a single cytoplasmic form of dynein carries out the functions of retrograde transport. To accomplish its tasks, dynein makes use of multiple subunits and accessory proteins, including heavy chains, light chains, intermediate chains, light intermediate chains, and dynactin to form a motor complex of several megadaltons. The last two thirds of the dynein heavy chains contain the main motor unit required for force production, while the N-terminal tail region of the dynein heavy chain along, with other dynein components, aid in cargo binding. Force production and microtubule-based movement is accomplished by coordinating ATP hydrolysis in the motor heads with a microtubule-binding domain. The tail domain allows for both homodimerization of motor heads as well as binding of other dynein subunits. In this work, various genetic, cell biology, and biochemical methods were used to study cytoplasmic dynein in the filamentous fungus, Neurospora crassa. Numerous dynein heavy chain mutants were isolated previously from a genetic screen, with a subset located to the C-terminal region, which were the focal point of this work. To explore the mechanism by which these mutations affect dynein function, both intragenic and extragenic suppressors were identified. A novel extragenic suppressor of dynein mutations was discovered, a gene encoding a putative E3 ubiquitin ligase with homologs present in higher organisms, including humans. Mutation or deletion of the suppressor gene results in restoration of wild type-like growth and in vivo dynein localization for each of the C-terminal dynein heavy chain mutants, as well as certain other dynein heavy chain mutants. Results suggest that the activity of this protein affects interaction of dynein heavy chain with dynein intermediate chain and likely is a regulator of dynein motor assembly. en_US
dc.description.tableofcontents Introduction -- Materials and methods -- Results -- Discussion en
dc.format.extent 144 pages en
dc.language.iso en_US en_US
dc.publisher University of Missouri--Kansas City en
dc.subject.lcsh Dynein en
dc.subject.lcsh Neurospora crassa en
dc.subject.mesh Ubiquitin-Protein Ligases en
dc.subject.other Dissertation -- University of Missouri--Kansas City -- Biology en
dc.title Involvement of a specific ubiquitin ligase in the assembly of the dynein motor in the filamentous fungus Neurospora crassa en_US
dc.type Thesis en_US
thesis.degree.discipline Cell Biology and Biophysics and Molecular Biology and Biochemistry en
thesis.degree.grantor University of Missouri--Kansas City en
thesis.degree.name Ph.D. en
thesis.degree.level Doctoral en


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