{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/83627"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/83627","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Biochemical and Genetic Studies on Origin Recognition and DNA Synthesis From the Mesophilic Archaeon Methanosarcina Acetivorans","abstract":"In our study, we characterized DinB and found that DinB was able to synthesize through abasic DNA and cyclobutane pyrimidine dimers, and these activities were stimulated by the cognate PCNA. Fascinatingly, unlike most translesion DNA polymerases previously described, MacDinB synthesized an unusually long product (∼7.2 kb) in the presence of the sliding clamp. A PCNA-interacting peptide (PIP) box located at the C-terminus of MacDinB was shown to facilitate interaction with the sliding clamp. Furthermore, individual mutations at different positions in the PIP-box led to identification of residues that are critical to PCNA/DinB interactions. Nevertheless, the biochemical analysis described here for DinB provides important insights into the properties, potential, and diversity of the Y-family of DNA polymerases.","abstract_html":"In our study, we characterized DinB and found that DinB was able to synthesize through abasic DNA and cyclobutane pyrimidine dimers, and these activities were stimulated by the cognate PCNA. Fascinatingly, unlike most translesion DNA polymerases previously described, MacDinB synthesized an unusually long product (∼7.2 kb) in the presence of the sliding clamp. A PCNA-interacting peptide (PIP) box located at the C-terminus of MacDinB was shown to facilitate interaction with the sliding clamp. Furthermore, individual mutations at different positions in the PIP-box led to identification of residues that are critical to PCNA/DinB interactions. Nevertheless, the biochemical analysis described here for DinB provides important insights into the properties, potential, and diversity of the Y-family of DNA polymerases.","abstract_has_math":false,"creators":["Lin, Li-Jung"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Animal Sciences","degree_department":null,"school":null,"contributors":["Isaac Cann"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T21:08:30Z","date_published":"2015-09-25T21:08:30Z","updated_at":"2026-07-22T22:26:21Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3392194"],"render_values":[{"text":"(MiAaPQ)AAI3392194","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/83627","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Isaac Cann"]},{"key":"dc:creator","label":"Author","values":["Lin, Li-Jung"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T21:08:30Z","10000-01-01","2009"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Animal Sciences"]},{"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/2142/83627","(MiAaPQ)AAI3392194"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In our study, we characterized DinB and found that DinB was able to synthesize through abasic DNA and cyclobutane pyrimidine dimers, and these activities were stimulated by the cognate PCNA. Fascinatingly, unlike most translesion DNA polymerases previously described, MacDinB synthesized an unusually long product (∼7.2 kb) in the presence of the sliding clamp. A PCNA-interacting peptide (PIP) box located at the C-terminus of MacDinB was shown to facilitate interaction with the sliding clamp. Furthermore, individual mutations at different positions in the PIP-box led to identification of residues that are critical to PCNA/DinB interactions. Nevertheless, the biochemical analysis described here for DinB provides important insights into the properties, potential, and diversity of the Y-family of DNA polymerases.","Made available in DSpace on 2015-09-25T21:08:30Z (GMT). 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Fascinatingly, unlike most translesion DNA polymerases previously described, MacDinB synthesized an unusually long product (∼7.2 kb) in the presence of the sliding clamp. A PCNA-interacting peptide (PIP) box located at the C-terminus of MacDinB was shown to facilitate interaction with the sliding clamp. Furthermore, individual mutations at different positions in the PIP-box led to identification of residues that are critical to PCNA/DinB interactions. Nevertheless, the biochemical analysis described here for DinB provides important insights into the properties, potential, and diversity of the Y-family of DNA polymerases.","Made available in DSpace on 2015-09-25T21:08:30Z (GMT). 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