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Human La's Nuclear Retention Element Functions in La-RNA Target Discrimination

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dc.contributor.advisorBayfield, Mark
dc.creatorMarrella, Stefano Alessandro
dc.date.accessioned2018-03-01T14:03:33Z
dc.date.available2018-03-01T14:03:33Z
dc.date.copyright2017-08-08
dc.date.issued2018-03-01
dc.date.updated2018-03-01T14:03:32Z
dc.degree.disciplineBiology
dc.degree.levelMaster's
dc.degree.nameMSc - Master of Science
dc.description.abstractThe La protein is an abundant RNA processing protein located in the nucleus of eukaryotic cells. Removal of the -helical nuclear retention element domain in human La causes the inappropriate export of these hLa-NRE mutants from the nucleus, resulting in the accumulation of non-functional aberrantly processed tRNAs within the cytoplasm. We hypothesized that the inappropriate nuclear export of hLa-NRE may be an indirect consequence of altered RNA target binding in cells. Electrophoretic mobility shift assays revealed hLa-NRE mutants exhibiting diminished binding affinity for precursor tRNAs in comparison to wild-type human La, however no differences in affinity were seen with poly A target binding. From this, we proposed a hypothetical model which suggests the cause for export of hLa-NRE mutants is a result of competitive binding with mRNA targets in the nucleus. This competition for binding results in the inappropriate export of these mutants with mRNA targets in a crm1-dependant manner.
dc.identifier.urihttp://hdl.handle.net/10315/34352
dc.language.isoen
dc.rightsAuthor owns copyright, except where explicitly noted. Please contact the author directly with licensing requests.
dc.subjectMolecular biology
dc.subject.keywordshLa
dc.subject.keywordsHuman La protein
dc.subject.keywordsLupus Autoantigen
dc.subject.keywordsSS-B
dc.subject.keywordsRNA Biology
dc.subject.keywordstRNA processing
dc.subject.keywordsNuclear retention element
dc.titleHuman La's Nuclear Retention Element Functions in La-RNA Target Discrimination
dc.typeElectronic Thesis or Dissertation

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