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Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion

Abstract

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.

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

Rights

Language dc:language
en

Identifiers

dc:identifier.*
OAI identifier oai:identifier
oai:tdl-ir.tdl.org:20.500.12503/29638

Chain of custody

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Texas Digital Library
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Last updated
2026-07-27
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citation

Perez-Lamigueiro, Maria A.. Changes in Mammalian Chromatin Structure as a Function of Protein-Poly(ADP-Ribosyl)ation by Endonuclease Digestion. 2004. https://hdl.handle.net/20.500.12503/29638