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Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion
Abstract
dc:description.abstractPerez-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.
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Perez-Lamigueiro, Maria A.
- Contributors dc:contributor
-
- Alvarez, Rafael
- Das, Hriday K.
- Basu, Alakananda
Subjects
dc:subject × 26- 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
Rights
- Language dc:language
- en
Identifiers
dc:identifier.*- Handle dc:identifier.uri
- https://hdl.handle.net/20.500.12503/29638
- OAI identifier oai:identifier
- oai:tdl-ir.tdl.org:20.500.12503/29638