{"id":{"repo_id":"unt","oai_identifier":"info:ark/67531/metadc3057"},"canonical_url":"https://search.dev.ndltd.org/etd/unt/info:ark/67531/metadc3057","repository":{"repo_id":"unt","name":"University of North Texas","base_url":"https://digital.library.unt.edu/oai/"},"display":{"title":"Characterization of the Aspartate Transcarbamoylase that is Found in the pyrBC\" Complex of Bordetella Pertussis","abstract":"An aspartate transcarbamoylase (ATCase) gene from Bordetella pertussis was amplified by PCR and ligated into pT-ADV for expression in Escherichia coli. This particular ATCase (pyrB) was an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was undertaken to determine whether this pyrB gene was capable of expression alone or if it was capable of expression only when cotransformed with a functional pyrC'. When transformed into E. coli TB2 pyrB-, the gene did not produce any ATCase activity. The gene was then co-transformed into E. coli TB2 pyrB- along with a plasmid containing the pyrC' gene from Pseudomonas aeruginosa and assayed for ATCase activity. Negative results were again recorded.","abstract_html":"An aspartate transcarbamoylase (ATCase) gene from Bordetella pertussis was amplified by PCR and ligated into pT-ADV for expression in Escherichia coli. This particular ATCase (pyrB) was an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was undertaken to determine whether this pyrB gene was capable of expression alone or if it was capable of expression only when cotransformed with a functional pyrC'. When transformed into E. coli TB2 pyrB-, the gene did not produce any ATCase activity. The gene was then co-transformed into E. coli TB2 pyrB- along with a plasmid containing the pyrC' gene from Pseudomonas aeruginosa and assayed for ATCase activity. Negative results were again recorded.","abstract_has_math":false,"creators":["Dill, Michael T"],"institution":"University of North Texas","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001-12","date_published":"2001-12","updated_at":"2026-07-24T05:34:52Z","subjects":["Pyrimidine nucleotides -- Metabolism.","Bordetella pertussis.","aspartate transcarbamoylase","Bordetella pertussis","ATCase","pyrBC complex","gene expression"],"languages":["English"],"rights":["Public","Copyright","Dill, Michael T","Copyright is held by the author, unless otherwise noted. All rights reserved."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 51977993","https://digital.library.unt.edu/ark:/67531/metadc3057/","ark: ark:/67531/metadc3057"],"render_values":[{"text":"oclc: 51977993","href":null,"code":true},{"text":"https://digital.library.unt.edu/ark:/67531/metadc3057/","href":"https://digital.library.unt.edu/ark:/67531/metadc3057/","code":true},{"text":"ark: ark:/67531/metadc3057","href":null,"code":true}]}]},"links":{"outbound_url":"https://doi.org/10.12794/metadc3057","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."]},{"key":"dc:creator","label":"Author","values":["Dill, Michael T"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2001-12"]},{"key":"dc:publisher","label":"Institution","values":["University of North Texas"]},{"key":"dc:type","label":"Dc Type","values":["Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Pyrimidine nucleotides -- Metabolism.","Bordetella pertussis.","aspartate transcarbamoylase","Bordetella pertussis","ATCase","pyrBC complex","gene expression"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["Public","Copyright","Dill, Michael T","Copyright is held by the author, unless otherwise noted. All rights reserved."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 51977993","doi: 10.12794/metadc3057","https://digital.library.unt.edu/ark:/67531/metadc3057/","ark: ark:/67531/metadc3057"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["An aspartate transcarbamoylase (ATCase) gene from Bordetella pertussis was amplified by PCR and ligated into pT-ADV for expression in Escherichia coli. This particular ATCase (pyrB) was an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was undertaken to determine whether this pyrB gene was capable of expression alone or if it was capable of expression only when cotransformed with a functional pyrC'. When transformed into E. coli TB2 pyrB-, the gene did not produce any ATCase activity. The gene was then co-transformed into E. coli TB2 pyrB- along with a plasmid containing the pyrC' gene from Pseudomonas aeruginosa and assayed for ATCase activity. Negative results were again recorded."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:title","label":"Title","values":["Characterization of the Aspartate Transcarbamoylase that is Found in the pyrBC\" Complex of Bordetella Pertussis"]}]}],"canonical_facts":{"dc:contributor":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."],"dc:creator":["Dill, Michael T"],"dc:date":["2001-12"],"dc:description":["An aspartate transcarbamoylase (ATCase) gene from Bordetella pertussis was amplified by PCR and ligated into pT-ADV for expression in Escherichia coli. This particular ATCase (pyrB) was an inactive gene found adjacent to an inactive dihydroorotase (DHOase) gene (pyrC'). This experiment was undertaken to determine whether this pyrB gene was capable of expression alone or if it was capable of expression only when cotransformed with a functional pyrC'. When transformed into E. coli TB2 pyrB-, the gene did not produce any ATCase activity. The gene was then co-transformed into E. coli TB2 pyrB- along with a plasmid containing the pyrC' gene from Pseudomonas aeruginosa and assayed for ATCase activity. Negative results were again recorded."],"dc:format":["Text"],"dc:identifier":["oclc: 51977993","doi: 10.12794/metadc3057","https://digital.library.unt.edu/ark:/67531/metadc3057/","ark: ark:/67531/metadc3057"],"dc:language":["English"],"dc:publisher":["University of North Texas"],"dc:rights":["Public","Copyright","Dill, Michael T","Copyright is held by the author, unless otherwise noted. All rights reserved."],"dc:subject":["Pyrimidine nucleotides -- Metabolism.","Bordetella pertussis.","aspartate transcarbamoylase","Bordetella pertussis","ATCase","pyrBC complex","gene expression"],"dc:title":["Characterization of the Aspartate Transcarbamoylase that is Found in the pyrBC\" Complex of Bordetella Pertussis"],"dc:type":["Thesis or Dissertation"]},"updated_at":"2026-07-24T05:34:52Z"}