{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86685"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86685","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"DNA -Protein Interactions in the CTnDOT Excisive Intasome","abstract":"The excision mechanism of CTnDOT is more complicated than any system studied to date. Excision requires multiple accessory proteins. Exc is one protein required for excision, however, its function is unknown. In an attempt to determine a role for Exc, the native wild type Exc protein was purified. These studies indicated that Exc might interact with IntDOT during excision, as determined by electrophoretic mobility shift assays. Further studies of Exc are warranted to answer the many questions that still remain about its function.","abstract_html":"The excision mechanism of CTnDOT is more complicated than any system studied to date. Excision requires multiple accessory proteins. Exc is one protein required for excision, however, its function is unknown. In an attempt to determine a role for Exc, the native wild type Exc protein was purified. These studies indicated that Exc might interact with IntDOT during excision, as determined by electrophoretic mobility shift assays. Further studies of Exc are warranted to answer the many questions that still remain about its function.","abstract_has_math":false,"creators":["Dichiara, Jeanne M."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Gardner, Jeffrey F."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:25Z","date_published":"2015-09-28T15:17:25Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3242833"],"render_values":[{"text":"(MiAaPQ)AAI3242833","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86685","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gardner, Jeffrey F."]},{"key":"dc:creator","label":"Author","values":["Dichiara, Jeanne M."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:25Z","10000-01-01","2006"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"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/2142/86685","(MiAaPQ)AAI3242833"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The excision mechanism of CTnDOT is more complicated than any system studied to date. Excision requires multiple accessory proteins. Exc is one protein required for excision, however, its function is unknown. In an attempt to determine a role for Exc, the native wild type Exc protein was purified. These studies indicated that Exc might interact with IntDOT during excision, as determined by electrophoretic mobility shift assays. Further studies of Exc are warranted to answer the many questions that still remain about its function.","Made available in DSpace on 2015-09-28T15:17:25Z (GMT). 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Exc is one protein required for excision, however, its function is unknown. In an attempt to determine a role for Exc, the native wild type Exc protein was purified. These studies indicated that Exc might interact with IntDOT during excision, as determined by electrophoretic mobility shift assays. Further studies of Exc are warranted to answer the many questions that still remain about its function.","Made available in DSpace on 2015-09-28T15:17:25Z (GMT). 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