{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84881"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84881","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Essential Glycosyltransferases in Schizosaccharomyces Pombe","abstract":"I cloned cDNAs encoding S. pombe, human and Caenorhabditis briggsiae Dol-P-Man synthases, all three of which lack a characteristic carboxy-terminal transmembrane region found on previously isolated Dol-P-Man synthases. Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.","abstract_html":"I cloned cDNAs encoding S. pombe, human and Caenorhabditis briggsiae Dol-P-Man synthases, all three of which lack a characteristic carboxy-terminal transmembrane region found on previously isolated Dol-P-Man synthases. Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.","abstract_has_math":true,"creators":["Colussi, Paul Attilio"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Peter A.B.Orlean"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:28:19Z","date_published":"2015-09-25T22:28:19Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9737080"],"render_values":[{"text":"(MiAaPQ)AAI9737080","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84881","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Peter A.B.Orlean"]},{"key":"dc:creator","label":"Author","values":["Colussi, Paul Attilio"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:19Z","10000-01-01","1997"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"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":["Biology, Microbiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84881","(MiAaPQ)AAI9737080"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["I cloned cDNAs encoding S. pombe, human and Caenorhabditis briggsiae Dol-P-Man synthases, all three of which lack a characteristic carboxy-terminal transmembrane region found on previously isolated Dol-P-Man synthases. Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.","Made available in DSpace on 2015-09-25T22:28:19Z (GMT). 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Known Dol-P-Man synthases can therefore be divided into a 'human' or 'S. cerevisiae' class, although the two are functionally equivalent for I showed that the S. cerevisiae DPM1 gene and its human counterpart both complement the lethal dpm1$\\sp+$ null mutation in S. pombe. The 'human' class of Dol-P-Man synthases, however, do not complement an S. cerevisiae dpm1 null mutant, and, unlike the S. cerevisiae class of enzymes, do not confer Dol-P-Man synthetic activity on E. coli cells. I propose that the 'human' class of Dol-P-Man synthase requires one or more auxiliary proteins for catalytic activity or to mediate membrane association. The facts that Dol-P-Man synthase is an essential enzyme in yeast, and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme, raises the possibility that Dol-P-Man synthase could be exploited as a target for selective inhibitors of pathogenic eukaryotic microbes.","Made available in DSpace on 2015-09-25T22:28:19Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9737080.pdf: 5945140 bytes, checksum: 4d827825fa0f458b6867574161271555 (MD5) Previous issue date: 1997","Embargo set by: Seth Robbins for item 86162 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","147 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997."],"dc:identifier":["http://hdl.handle.net/2142/84881","(MiAaPQ)AAI9737080"],"dc:language":["eng"],"dc:subject":["Biology, Microbiology"],"dc:title":["Essential Glycosyltransferases in Schizosaccharomyces Pombe"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:24Z"}