{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70541"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70541","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Phosphatase Activities of T4 Polynucleotide Kinase (Rna Ligase, Splicing)","abstract":"The recent elucidation of the role of the 2':3'-cyclic phosphate in the mechanism of tRNA splicing in wheat germ and yeast prompted a closer examination of the 3'-phosphatase activity of T4 polynucleotide kinase. This resulted in the discovery of not only a 2':3'-cyclic phosphatase activity but also a 2'-phosphatase, in addition to the previously demonstrated 3'-phosphatase. The relationship between the three activities is characterized by determining the pH rate profile, kinetic constants for both ribonucleotide and deoxyribonucleotide substrates and length dependence of each activity. The data suggests that all three activities occur at the same active site. In addition, a model is proposed in which the 2':3'-cyclic phosphatase and kinase activities function with RNA ligase in tRNA breakage and religation.","abstract_html":"The recent elucidation of the role of the 2&#x27;:3&#x27;-cyclic phosphate in the mechanism of tRNA splicing in wheat germ and yeast prompted a closer examination of the 3&#x27;-phosphatase activity of T4 polynucleotide kinase. This resulted in the discovery of not only a 2&#x27;:3&#x27;-cyclic phosphatase activity but also a 2&#x27;-phosphatase, in addition to the previously demonstrated 3&#x27;-phosphatase. The relationship between the three activities is characterized by determining the pH rate profile, kinetic constants for both ribonucleotide and deoxyribonucleotide substrates and length dependence of each activity. The data suggests that all three activities occur at the same active site. In addition, a model is proposed in which the 2&#x27;:3&#x27;-cyclic phosphatase and kinase activities function with RNA ligase in tRNA breakage and religation.","abstract_has_math":false,"creators":["Weber, Thomas Richard"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-15T23:43:51Z","date_published":"2014-12-15T23:43:51Z","updated_at":"2026-07-22T22:26:03Z","subjects":["Chemistry, Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8511690"],"render_values":[{"text":"(UMI)AAI8511690","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70541","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Weber, Thomas Richard"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:43:51Z","10000-01-01","1985"]},{"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":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70541","(UMI)AAI8511690"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The recent elucidation of the role of the 2':3'-cyclic phosphate in the mechanism of tRNA splicing in wheat germ and yeast prompted a closer examination of the 3'-phosphatase activity of T4 polynucleotide kinase. This resulted in the discovery of not only a 2':3'-cyclic phosphatase activity but also a 2'-phosphatase, in addition to the previously demonstrated 3'-phosphatase. The relationship between the three activities is characterized by determining the pH rate profile, kinetic constants for both ribonucleotide and deoxyribonucleotide substrates and length dependence of each activity. The data suggests that all three activities occur at the same active site. In addition, a model is proposed in which the 2':3'-cyclic phosphatase and kinase activities function with RNA ligase in tRNA breakage and religation.","Made available in DSpace on 2014-12-15T23:43:51Z (GMT). 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This resulted in the discovery of not only a 2':3'-cyclic phosphatase activity but also a 2'-phosphatase, in addition to the previously demonstrated 3'-phosphatase. The relationship between the three activities is characterized by determining the pH rate profile, kinetic constants for both ribonucleotide and deoxyribonucleotide substrates and length dependence of each activity. The data suggests that all three activities occur at the same active site. In addition, a model is proposed in which the 2':3'-cyclic phosphatase and kinase activities function with RNA ligase in tRNA breakage and religation.","Made available in DSpace on 2014-12-15T23:43:51Z (GMT). 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