{"id":{"repo_id":"tdl","oai_identifier":"oai:tdl-ir.tdl.org:20.500.12503/29638"},"canonical_url":"https://search.dev.ndltd.org/etd/tdl/oai:tdl-ir.tdl.org:20.500.12503/29638","repository":{"repo_id":"tdl","name":"Texas Digital Library","base_url":"https://tdl-ir.tdl.org/server/oai/request"},"display":{"title":"Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion","abstract":"Perez-Lamiguerio, Maria A., Changes in Mammalian Chromatin Structure as a Function of Protein-poly(ADP-ribosyl)ation by Endonuclease Digestion. Master of Science (Biochemistry and Molecular Biology), June 2004. 66 pages, 12 illustrations, Bibliography, 45 titles. Mammalian chromatin was exposed to either Deoxyribonuclease I or Micrococcal Nuclease digestion as a function of time of incubation and enzyme concentration. Endonuclease enzymatic reactions were stopped with EDTA. Samples were run in 1.5% agarose gels and the oligonucleosomal electrophoretic migration patterns compared. Endonuclease experiments were carried out with rat liver chromatin pre-incubated in the presence or absence of 200 μM βNAD+. A solution of 1.0 mM benzamide was used to stop enzymatic modification. The electrophoretic observations demonstrated a faster and increased degradation of chromatin when proteins were poly(ADP-ribosyl)ated prior to digestion. These results support the hypothesis that that the covalent poly(ADP-ribosyl)ation of chromatin proteins, particularly histones, induces a more relaxed structure, rendering chromatin more sensitive to endonuclease digestion.","abstract_html":"Perez-Lamiguerio, Maria A., Changes in Mammalian Chromatin Structure as a Function of Protein-poly(ADP-ribosyl)ation by Endonuclease Digestion. Master of Science (Biochemistry and Molecular Biology), June 2004. 66 pages, 12 illustrations, Bibliography, 45 titles. Mammalian chromatin was exposed to either Deoxyribonuclease I or Micrococcal Nuclease digestion as a function of time of incubation and enzyme concentration. Endonuclease enzymatic reactions were stopped with EDTA. Samples were run in 1.5% agarose gels and the oligonucleosomal electrophoretic migration patterns compared. Endonuclease experiments were carried out with rat liver chromatin pre-incubated in the presence or absence of 200 μM βNAD+. A solution of 1.0 mM benzamide was used to stop enzymatic modification. The electrophoretic observations demonstrated a faster and increased degradation of chromatin when proteins were poly(ADP-ribosyl)ated prior to digestion. These results support the hypothesis that that the covalent poly(ADP-ribosyl)ation of chromatin proteins, particularly histones, induces a more relaxed structure, rendering chromatin more sensitive to endonuclease digestion.","abstract_has_math":false,"creators":["Perez-Lamigueiro, Maria A."],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Alvarez, Rafael","Das, Hriday K.","Basu, Alakananda"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2004,"date_issued":"2004-06-01","date_published":"2004-06-01","updated_at":"2026-07-27T21:19:06Z","subjects":["Cell Anatomy","Cell and Developmental Biology","Cell Biology","Cellular and Molecular Physiology","Computational Biology","Genetics","Genetics and Genomics","Genomics","Life Sciences","Medical Cell Biology","Medical Genetics","Medicine and Health Sciences","Molecular Genetics","Other Cell and Developmental Biology","Other Genetics and Genomics","Mammalian chromatin structure","function","poly(ADP-ribosyl)ation","endonuclease digestion","deoxyribonuclease","micrococcal nuclease digestion","enzymatic reactions","EDTA","rat liver chromatin","proteins","histones"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/20.500.12503/29638","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Alvarez, Rafael","Das, Hriday K.","Basu, Alakananda"]},{"key":"dc:creator","label":"Author","values":["Perez-Lamigueiro, Maria A."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-08-22T21:51:56Z","2026-03-24T17:15:08Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2019-08-22T21:51:56Z"]},{"key":"dc:date.issued","label":"Date","values":["2004-06-01"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Cell Anatomy","Cell and Developmental Biology","Cell Biology","Cellular and Molecular Physiology","Computational Biology","Genetics","Genetics and Genomics","Genomics","Life Sciences","Medical Cell Biology","Medical Genetics","Medicine and Health Sciences","Molecular Genetics","Other Cell and Developmental Biology","Other Genetics and Genomics","Mammalian chromatin structure","function","poly(ADP-ribosyl)ation","endonuclease digestion","deoxyribonuclease","micrococcal nuclease digestion","enzymatic reactions","EDTA","rat liver chromatin","proteins","histones"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/20.500.12503/29638"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/20.500.12503/29638"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Perez-Lamiguerio, Maria A., Changes in Mammalian Chromatin Structure as a Function of Protein-poly(ADP-ribosyl)ation by Endonuclease Digestion. 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These results support the hypothesis that that the covalent poly(ADP-ribosyl)ation of chromatin proteins, particularly histones, induces a more relaxed structure, rendering chromatin more sensitive to endonuclease digestion."]},{"key":"dc:title","label":"Title","values":["Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion"]}]}],"canonical_facts":{"dc:contributor":["Alvarez, Rafael","Das, Hriday K.","Basu, Alakananda"],"dc:creator":["Perez-Lamigueiro, Maria A."],"dc:date.accessioned":["2019-08-22T21:51:56Z","2026-03-24T17:15:08Z"],"dc:date.available":["2019-08-22T21:51:56Z"],"dc:date.issued":["2004-06-01"],"dc:description.abstract":["Perez-Lamiguerio, Maria A., Changes in Mammalian Chromatin Structure as a Function of Protein-poly(ADP-ribosyl)ation by Endonuclease Digestion. Master of Science (Biochemistry and Molecular Biology), June 2004. 66 pages, 12 illustrations, Bibliography, 45 titles. Mammalian chromatin was exposed to either Deoxyribonuclease I or Micrococcal Nuclease digestion as a function of time of incubation and enzyme concentration. Endonuclease enzymatic reactions were stopped with EDTA. Samples were run in 1.5% agarose gels and the oligonucleosomal electrophoretic migration patterns compared. Endonuclease experiments were carried out with rat liver chromatin pre-incubated in the presence or absence of 200 μM βNAD+. A solution of 1.0 mM benzamide was used to stop enzymatic modification. The electrophoretic observations demonstrated a faster and increased degradation of chromatin when proteins were poly(ADP-ribosyl)ated prior to digestion. 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