{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84842"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84842","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The P22 Xis Protein: Regulation of Bacteriophage P22 Site -Specific Recombination","abstract":"Mutants of P22 Xis were isolated and assayed for excision system in vivo, to quantify their excision activity relative to wild-type Xis. Mutants S18F, R19A, G29S, G29D, A33P, R35C, D37G, S43F, S43P, P44L, L46F, A51T, and A51V were found to be defective in stimulating excision. Additionally, truncation mutants S66Z, K76Z, and D97Z were decreased in function about five-fold. In contrast, truncation mutants Q57Z and a mutant with the first 21 amino acids deleted were completely defective. Substitution mutants at R105, K107, and R109 revealed that this region stimulates the reactaion. A subset of Xis mutants were purified and assayed by EMSA and crosslinking studies. All purified mutants formed multimers by crosslinking, but L15F, K16E, A33P, S43F, and A55T were defective in DNA binding. Furthermore, L46F bound DNA with a weaker affinity but still formed specific complexes.","abstract_html":"Mutants of P22 Xis were isolated and assayed for excision system in vivo, to quantify their excision activity relative to wild-type Xis. Mutants S18F, R19A, G29S, G29D, A33P, R35C, D37G, S43F, S43P, P44L, L46F, A51T, and A51V were found to be defective in stimulating excision. Additionally, truncation mutants S66Z, K76Z, and D97Z were decreased in function about five-fold. In contrast, truncation mutants Q57Z and a mutant with the first 21 amino acids deleted were completely defective. Substitution mutants at R105, K107, and R109 revealed that this region stimulates the reactaion. A subset of Xis mutants were purified and assayed by EMSA and crosslinking studies. All purified mutants formed multimers by crosslinking, but L15F, K16E, A33P, S43F, and A55T were defective in DNA binding. Furthermore, L46F bound DNA with a weaker affinity but still formed specific complexes.","abstract_has_math":false,"creators":["Mattis, Aras Nikodemas"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Gumport, Richard I."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:28:09Z","date_published":"2015-09-25T22:28:09Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3290313"],"render_values":[{"text":"(MiAaPQ)AAI3290313","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84842","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gumport, Richard I."]},{"key":"dc:creator","label":"Author","values":["Mattis, Aras Nikodemas"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:09Z","10000-01-01","2007"]},{"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":["Chemistry, Biochemistry"]}]},{"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/2142/84842","(MiAaPQ)AAI3290313"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Mutants of P22 Xis were isolated and assayed for excision system in vivo, to quantify their excision activity relative to wild-type Xis. Mutants S18F, R19A, G29S, G29D, A33P, R35C, D37G, S43F, S43P, P44L, L46F, A51T, and A51V were found to be defective in stimulating excision. Additionally, truncation mutants S66Z, K76Z, and D97Z were decreased in function about five-fold. In contrast, truncation mutants Q57Z and a mutant with the first 21 amino acids deleted were completely defective. Substitution mutants at R105, K107, and R109 revealed that this region stimulates the reactaion. A subset of Xis mutants were purified and assayed by EMSA and crosslinking studies. All purified mutants formed multimers by crosslinking, but L15F, K16E, A33P, S43F, and A55T were defective in DNA binding. Furthermore, L46F bound DNA with a weaker affinity but still formed specific complexes.","Made available in DSpace on 2015-09-25T22:28:09Z (GMT). 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Mutants S18F, R19A, G29S, G29D, A33P, R35C, D37G, S43F, S43P, P44L, L46F, A51T, and A51V were found to be defective in stimulating excision. Additionally, truncation mutants S66Z, K76Z, and D97Z were decreased in function about five-fold. In contrast, truncation mutants Q57Z and a mutant with the first 21 amino acids deleted were completely defective. Substitution mutants at R105, K107, and R109 revealed that this region stimulates the reactaion. A subset of Xis mutants were purified and assayed by EMSA and crosslinking studies. All purified mutants formed multimers by crosslinking, but L15F, K16E, A33P, S43F, and A55T were defective in DNA binding. Furthermore, L46F bound DNA with a weaker affinity but still formed specific complexes.","Made available in DSpace on 2015-09-25T22:28:09Z (GMT). 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