{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/50420"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/50420","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The role of the Dgk1 and Pah1 in lipid interconversion on saccharomyces cerevisiae vacuole physiology, homeostasis, protein sorting and fusion","abstract":"A variety of factors are needed for the homotypic fusion of the yeast vacuole, including a number of proteins and regulatory lipids. The deletion of the phosphatidic acid (PA) phosphatase gene Pah1, which converts PA in diacylglycerol kinase (DAG), was previously shown to produce a fragmented vacuole phenotype, greatly inhibit fusion and result in the vacuolar protein sorting defect. As such, the impact of the deletion of the complementary DAG kinase gene Dgk1, which converts DAG into PA, and the impact of deleting both genes was observed. The deletion of Dgk1 was observed to augment fusion, despite showing a moderately fragmented vacuolar phenotype. This fusion was shown to still be dependent on the core fusion machinery proteins, and resistant to inhibition by the DAG ligand C1B, and was better able to maintain fusion capacity when held for an extended time on ice. This deletion also had a unique protein profile, different from the wild type background, but not the inverse of the Pah1 deletion. The double deletion showed highly fragmented vacuoles, much like Pah1 deletion, though these vacuoles were able to reform after osmotic shock, similar to the wild type background, but unlike either single deletion strain. This strain displayed reduced fusion and, interestingly, what appeared to be either the aberrant production, or degradation, of proteins. This observation points to a potentially more global cause for the observed phenotypes.","abstract_html":"A variety of factors are needed for the homotypic fusion of the yeast vacuole, including a number of proteins and regulatory lipids. The deletion of the phosphatidic acid (PA) phosphatase gene Pah1, which converts PA in diacylglycerol kinase (DAG), was previously shown to produce a fragmented vacuole phenotype, greatly inhibit fusion and result in the vacuolar protein sorting defect. As such, the impact of the deletion of the complementary DAG kinase gene Dgk1, which converts DAG into PA, and the impact of deleting both genes was observed. The deletion of Dgk1 was observed to augment fusion, despite showing a moderately fragmented vacuolar phenotype. This fusion was shown to still be dependent on the core fusion machinery proteins, and resistant to inhibition by the DAG ligand C1B, and was better able to maintain fusion capacity when held for an extended time on ice. This deletion also had a unique protein profile, different from the wild type background, but not the inverse of the Pah1 deletion. The double deletion showed highly fragmented vacuoles, much like Pah1 deletion, though these vacuoles were able to reform after osmotic shock, similar to the wild type background, but unlike either single deletion strain. This strain displayed reduced fusion and, interestingly, what appeared to be either the aberrant production, or degradation, of proteins. This observation points to a potentially more global cause for the observed phenotypes.","abstract_has_math":false,"creators":["Stoy, Colin"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Fratti, Rutilio A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-09-16T17:12:48Z","date_published":"2014-09-16T17:12:48Z","updated_at":"2026-07-22T22:25:40Z","subjects":["Diacylglycerol","Diacylglycerol Kinase","Phosphatidic Acid","Phosphatidic Acid Phosphatase","Saccharomyces Cerevisiae","Vacuole Fusion","Vacuole Homeostasis","Protein Sorting","Lipid Interconversion"],"languages":["en"],"rights":["Copyright 2014 Colin Stoy"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/50420","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Fratti, Rutilio A."]},{"key":"dc:creator","label":"Author","values":["Stoy, Colin"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-09-16T17:12:48Z","2016-09-22T20:59:16Z","2014-08","2014-09-16"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Diacylglycerol","Diacylglycerol Kinase","Phosphatidic Acid","Phosphatidic Acid Phosphatase","Saccharomyces Cerevisiae","Vacuole Fusion","Vacuole Homeostasis","Protein Sorting","Lipid Interconversion"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2014 Colin Stoy"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/50420"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["A variety of factors are needed for the homotypic fusion of the yeast vacuole, including a number of proteins and regulatory lipids. The deletion of the phosphatidic acid (PA) phosphatase gene Pah1, which converts PA in diacylglycerol kinase (DAG), was previously shown to produce a fragmented vacuole phenotype, greatly inhibit fusion and result in the vacuolar protein sorting defect. As such, the impact of the deletion of the complementary DAG kinase gene Dgk1, which converts DAG into PA, and the impact of deleting both genes was observed. The deletion of Dgk1 was observed to augment fusion, despite showing a moderately fragmented vacuolar phenotype. This fusion was shown to still be dependent on the core fusion machinery proteins, and resistant to inhibition by the DAG ligand C1B, and was better able to maintain fusion capacity when held for an extended time on ice. This deletion also had a unique protein profile, different from the wild type background, but not the inverse of the Pah1 deletion. The double deletion showed highly fragmented vacuoles, much like Pah1 deletion, though these vacuoles were able to reform after osmotic shock, similar to the wild type background, but unlike either single deletion strain. This strain displayed reduced fusion and, interestingly, what appeared to be either the aberrant production, or degradation, of proteins. This observation points to a potentially more global cause for the observed phenotypes.","Item withdrawn by Laura Spradlin (lspradl2@illinois.edu) on 2014-07-25T17:12:33Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 2 Stoy_Colin.doc: 1014784 bytes, checksum: 5e53078ebadfd001a8e8a26bc08636c5 (MD5) Stoy_Colin.pdf: 505178 bytes, checksum: 7e24c1d93c27f1aa72e2d03c8a478402 (MD5)","Made available in DSpace on 2014-09-16T17:12:48Z (GMT). No. of bitstreams: 3 Colin_Stoy.pdf: 513380 bytes, checksum: aec5d69ea0237a2dedc7f89bd5ad9c3c (MD5) Stoy_Colin.doc: 1013760 bytes, checksum: 37270e04ee382e7ce5445b23bbda6b72 (MD5) license.txt: 4058 bytes, checksum: f6a6ad75066229ac6d437456d149e6a3 (MD5)","Embargo set by: Seth Robbins for item 50531 Lift date: 2016-09-16T17:13:01Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited Restriction Lifted for Item 50531 on 2016-09-22T20:59:16Z."]},{"key":"dc:title","label":"Title","values":["The role of the Dgk1 and Pah1 in lipid interconversion on saccharomyces cerevisiae vacuole physiology, homeostasis, protein sorting and fusion"]}]}],"canonical_facts":{"dc:contributor":["Fratti, Rutilio A."],"dc:creator":["Stoy, Colin"],"dc:date":["2014-09-16T17:12:48Z","2016-09-22T20:59:16Z","2014-08","2014-09-16"],"dc:description":["A variety of factors are needed for the homotypic fusion of the yeast vacuole, including a number of proteins and regulatory lipids. The deletion of the phosphatidic acid (PA) phosphatase gene Pah1, which converts PA in diacylglycerol kinase (DAG), was previously shown to produce a fragmented vacuole phenotype, greatly inhibit fusion and result in the vacuolar protein sorting defect. As such, the impact of the deletion of the complementary DAG kinase gene Dgk1, which converts DAG into PA, and the impact of deleting both genes was observed. The deletion of Dgk1 was observed to augment fusion, despite showing a moderately fragmented vacuolar phenotype. This fusion was shown to still be dependent on the core fusion machinery proteins, and resistant to inhibition by the DAG ligand C1B, and was better able to maintain fusion capacity when held for an extended time on ice. This deletion also had a unique protein profile, different from the wild type background, but not the inverse of the Pah1 deletion. The double deletion showed highly fragmented vacuoles, much like Pah1 deletion, though these vacuoles were able to reform after osmotic shock, similar to the wild type background, but unlike either single deletion strain. This strain displayed reduced fusion and, interestingly, what appeared to be either the aberrant production, or degradation, of proteins. This observation points to a potentially more global cause for the observed phenotypes.","Item withdrawn by Laura Spradlin (lspradl2@illinois.edu) on 2014-07-25T17:12:33Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 2 Stoy_Colin.doc: 1014784 bytes, checksum: 5e53078ebadfd001a8e8a26bc08636c5 (MD5) Stoy_Colin.pdf: 505178 bytes, checksum: 7e24c1d93c27f1aa72e2d03c8a478402 (MD5)","Made available in DSpace on 2014-09-16T17:12:48Z (GMT). No. of bitstreams: 3 Colin_Stoy.pdf: 513380 bytes, checksum: aec5d69ea0237a2dedc7f89bd5ad9c3c (MD5) Stoy_Colin.doc: 1013760 bytes, checksum: 37270e04ee382e7ce5445b23bbda6b72 (MD5) license.txt: 4058 bytes, checksum: f6a6ad75066229ac6d437456d149e6a3 (MD5)","Embargo set by: Seth Robbins for item 50531 Lift date: 2016-09-16T17:13:01Z Reason: Author requested closed access (OA after 2yrs) in Vireo ETD system","Limited Restriction Lifted for Item 50531 on 2016-09-22T20:59:16Z."],"dc:identifier":["http://hdl.handle.net/2142/50420"],"dc:language":["en"],"dc:rights":["Copyright 2014 Colin Stoy"],"dc:subject":["Diacylglycerol","Diacylglycerol Kinase","Phosphatidic Acid","Phosphatidic Acid Phosphatase","Saccharomyces Cerevisiae","Vacuole Fusion","Vacuole Homeostasis","Protein Sorting","Lipid Interconversion"],"dc:title":["The role of the Dgk1 and Pah1 in lipid interconversion on saccharomyces cerevisiae vacuole physiology, homeostasis, protein sorting and fusion"],"dc:type":["text"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:40Z"}