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dc.contributor.advisorDieckmann, Carolen
dc.contributor.advisorMcEvoy, Meganen
dc.contributor.authorBroadfoot, Jourdan Elizabeth
dc.contributor.authorDieckmann, Carol
dc.creatorBroadfoot, Jourdan Elizabethen
dc.creatorDieckmann, Carolen
dc.date.accessioned2015-09-29T18:24:29Zen
dc.date.available2015-09-29T18:24:29Zen
dc.date.issued2015en
dc.identifier.urihttp://hdl.handle.net/10150/578883en
dc.description.abstractIn yeast mitochondria, the enzyme Lip3 is involved in the transfer of octanoic acid from Gcv3, a subunit of GCV, to other targets. However, it is unknown whether Lip3 itself has acyl transferase activity, or if it serves to present the fatty acid as well as the substrate to a transferase. When Lip3 is purified by tandem tag chromatography, the final eluate contains Lip3 as well as an additional co-purifying protein. It was hypothesized that this protein may be the transferase that Lip3 associates with when transferring octanoic acid. Furthermore, based on the size and predicted properties of this co-purifying protein, it was hypothesized that Yer087w may be the transferase that co-purifies with Lip3. However, when the YER087w gene was deleted in a yeast strain where Lip3 was tagged with Protein C peptide and His-6 (notated as Lip3- CH), the co-purifying protein was still present in the final eluate, indicating that Yer087w is not that protein. This was confirmed by mass spectrometry, which determined the co-purifying protein to be Heat Shock Protein 60.
dc.language.isoen_USen
dc.publisherThe University of Arizona.en
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en
dc.titleIs Yer087w Protein in Complex with Lip3, Functioning in Lipoylation in Yeast Mitochondria?en_US
dc.typetexten
dc.typeElectronic Thesisen
thesis.degree.grantorUniversity of Arizonaen
thesis.degree.levelbachelorsen
thesis.degree.disciplineHonors Collegeen
thesis.degree.disciplineBiochemistryen
thesis.degree.nameB.S.en
refterms.dateFOA2018-09-10T12:06:31Z
html.description.abstractIn yeast mitochondria, the enzyme Lip3 is involved in the transfer of octanoic acid from Gcv3, a subunit of GCV, to other targets. However, it is unknown whether Lip3 itself has acyl transferase activity, or if it serves to present the fatty acid as well as the substrate to a transferase. When Lip3 is purified by tandem tag chromatography, the final eluate contains Lip3 as well as an additional co-purifying protein. It was hypothesized that this protein may be the transferase that Lip3 associates with when transferring octanoic acid. Furthermore, based on the size and predicted properties of this co-purifying protein, it was hypothesized that Yer087w may be the transferase that co-purifies with Lip3. However, when the YER087w gene was deleted in a yeast strain where Lip3 was tagged with Protein C peptide and His-6 (notated as Lip3- CH), the co-purifying protein was still present in the final eluate, indicating that Yer087w is not that protein. This was confirmed by mass spectrometry, which determined the co-purifying protein to be Heat Shock Protein 60.


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