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dc.contributor.advisorBennett, Karen L.eng
dc.contributor.authorBeshore, Erica Leigh, 1982-eng
dc.date.issued2010eng
dc.date.submitted2010 Springeng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.descriptionTitle from PDF of title page (University of Missouri--Columbia, viewed on August 3, 2010).eng
dc.descriptionIncludes bibliographical referenceseng
dc.descriptionVita.eng
dc.descriptionThesis advisor: Karen Bennett.eng
dc.description"May 2010"eng
dc.descriptionPh. D. University of Missouri-Columbia 2010.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- microbiology (Medicine).eng
dc.description.abstractP granules are ribonucleoprotein complexes specific to the cytoplasmic side of the nuclear pores of C. elegans germ cells. While P granules are implicated in post-transcriptional control of maternally-transcribed mRNAs, their function remains elusive. Our laboratory is particularly interested in the P-granule component GLH-1 (Germline RNA Helicase-1). Through genetic studies our laboratory has shown that GLH-1 is essential for fertility; however, the biochemical function of the GLH complex is still unknown. With immunoprecipitations and GST-pulldowns, we report that GLH-1 and the riboendonuclease Dicer bind one another and their interaction is not RNA dependent. Both GLH-1 protein and mRNA levels are reduced in the dcr- 1(ok247) mutant background; conversely, a reduction of DCR-1 protein in the glh-1(gk100) deletion strain is also observed. Thus, in complex in the C. elegans germline, these two proteins seem interdependent. In addition, evidence indicates Dicer protein levels, like those of GLH-1, are regulated by proteosomal degradation and are much increased when the Jun N-terminal kinase KGB-1 is missing in the kgb-1(um3) null. In the adult C. elegans germline DCR-1 is located throughout the cytoplasm as well as at the inner nuclear pores of the germ cell nuclei, in close opposition to GLH-1. Under stress conditions in oocytes GLH-1 and DCR-1 both re-locate and recruit other components to large cytoplasmic RNP granules. We hypothesize the GLH-1/DCR-1 complex may function in the transport, deposition, or regulation of maternally-transcribed mRNAs perhaps with their associated miRNAs.eng
dc.format.extentxiii, 168 pageseng
dc.identifier.merlinb77429783eng
dc.identifier.merlinb77429783eng
dc.identifier.oclc653299332eng
dc.identifier.urihttps://hdl.handle.net/10355/8295
dc.identifier.urihttps://doi.org/10.32469/10355/8295eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartof2010 Freely available dissertations (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2010 Dissertationseng
dc.subject.meshRibonuclease III -- metabolismeng
dc.subject.meshDEAD-box RNA Helicases -- metabolismeng
dc.subject.meshRibonucleoproteins -- metabolismeng
dc.subject.meshCaenorhabditis elegans -- geneticseng
dc.subject.meshCaenorhabditis elegans -- physiologyeng
dc.subject.meshCaenorhabditis elegans Proteins -- metabolismeng
dc.subject.meshJNK Mitogen-Activated Protein Kinases -- metabolismeng
dc.subject.meshCytoplasmic Granules -- metabolismeng
dc.subject.meshRNA, Messengereng
dc.subject.meshGerm Cellseng
dc.titleDicer interacts with the P-granule component GLH-1: both localize to C. elegans nuclear pores and to stress-induced oocyte RNP granuleseng
dc.typeThesiseng
thesis.degree.disciplineMicrobiology (Medicine) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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