Influence of Peroxisomal Import and Receptor Recycling of Peroxisomal Function

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dc.contributor.advisorBartel, Bonnie
dc.creatorRatzel, Sarah E.
dc.date.accessioned2013-03-08T00:37:55Z
dc.date.available2013-03-08T00:37:55Z
dc.date.issued2011
dc.description.abstractPeroxisomes compartmentalize a variety of important metabolic reactions including fatty acid β-oxidation and the related process of IBA β-oxidation. Peroxisomal proteins are encoded by nuclear genes and must be post-translationally imported. A dynamic import process is vital for proper matrix protein localization and is dependent on the family of peroxin (PEX) proteins. The delivery and peroxisomal import of cargo from a loaded receptor, PEX5 or PEX7, is carried out by the early-acting peroxins, including PEX13 and PEX14, and receptor recycling is carried out by the late-acting peroxins, including PEX4 and PEX6. In this thesis, I describe the use of double mutant analysis to differentiate early-acting and late-acting pex mutants by phenotypic and molecular analysis. I found that double mutants made with two early-acting or two late-acting pex mutants showed enhanced phenotypes in β-oxidation and import defects. In contrast, defects of double mutants made with a weak early-acting mutant and a late-acting mutant were suppressed. Additionally, I found that receptor localization is central to proper peroxisomal function. My results suggest that when the receptor is not removed from the peroxisome, stabilized peroxisomal pores may be formed, perhaps impairing peroxisomal function due to leaching of peroxisomal contents. Together my data suggest that balance between import and receptor recycling is fundamental for peroxisomal function. In humans, peroxisomal biogenesis disorders are most often caused by defects in late-acting peroxins. Peroxisomal defects occur in plants and humans as a result of the same lesions in PEX proteins. The understanding of how these late-acting defects can be ameliorated in plants, may inspire new approaches to human therapeutics.
dc.format.extent127 p.en_US
dc.format.mimetypeapplication/pdf
dc.identifier.callnoTHESIS BIOCHEM. 2011 RATZEL
dc.identifier.citationRatzel, Sarah E.. "Influence of Peroxisomal Import and Receptor Recycling of Peroxisomal Function." (2011) Diss., Rice University. <a href="https://hdl.handle.net/1911/70403">https://hdl.handle.net/1911/70403</a>.
dc.identifier.digitalRatzelSen_US
dc.identifier.urihttps://hdl.handle.net/1911/70403
dc.language.isoeng
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.
dc.subjectPure sciences
dc.subjectBiological sciences
dc.subjectPeroxisomes
dc.subjectPeroxin proteins
dc.subjectReceptor recycling
dc.subjectGenetics
dc.subjectCellular biology
dc.subjectBiochemistry
dc.titleInfluence of Peroxisomal Import and Receptor Recycling of Peroxisomal Function
dc.typeThesis
dc.type.materialText
thesis.degree.departmentBiochemistry and Cell Biology
thesis.degree.disciplineNatural Sciences
thesis.degree.grantorRice University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy
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