Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion
dc.contributor.advisor | Alvarez, Rafael | |
dc.contributor.committeeMember | Das, Hriday K. | |
dc.contributor.committeeMember | Basu, Alakananda | |
dc.creator | Perez-Lamigueiro, Maria A. | |
dc.date.accessioned | 2019-08-22T21:51:56Z | |
dc.date.available | 2019-08-22T21:51:56Z | |
dc.date.issued | 2004-06-01 | |
dc.date.submitted | 2014-03-19T06:24:05-07:00 | |
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. 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. | |
dc.format.mimetype | application/pdf | |
dc.identifier.uri | https://hdl.handle.net/20.500.12503/29638 | |
dc.language.iso | en | |
dc.provenance.legacyDownloads | 0 | |
dc.subject | Cell Anatomy | |
dc.subject | Cell and Developmental Biology | |
dc.subject | Cell Biology | |
dc.subject | Cellular and Molecular Physiology | |
dc.subject | Computational Biology | |
dc.subject | Genetics | |
dc.subject | Genetics and Genomics | |
dc.subject | Genomics | |
dc.subject | Life Sciences | |
dc.subject | Medical Cell Biology | |
dc.subject | Medical Genetics | |
dc.subject | Medicine and Health Sciences | |
dc.subject | Molecular Genetics | |
dc.subject | Other Cell and Developmental Biology | |
dc.subject | Other Genetics and Genomics | |
dc.subject | Mammalian chromatin structure | |
dc.subject | function | |
dc.subject | poly(ADP-ribosyl)ation | |
dc.subject | endonuclease digestion | |
dc.subject | deoxyribonuclease | |
dc.subject | micrococcal nuclease digestion | |
dc.subject | enzymatic reactions | |
dc.subject | EDTA | |
dc.subject | rat liver chromatin | |
dc.subject | proteins | |
dc.subject | histones | |
dc.title | Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion | |
dc.type | Thesis | |
dc.type.material | text | |
thesis.degree.department | Graduate School of Biomedical Sciences | |
thesis.degree.discipline | Biochemistry and Molecular Biology | |
thesis.degree.grantor | University of North Texas Health Science Center at Fort Worth | |
thesis.degree.name | Master of Science |
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