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Title: Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin

Abstract

Poly (ADP-Ribose) Polymerase I (PARP-1) is a first responder to DNA damage and participates in the regulation of gene expression. The interaction of PARP-1 with chromatin and DNA is complex and involves at least two different modes of interaction. In its enzymatically inactive state, PARP-1 binds native chromatin with similar affinity as it binds free DNA ends. Automodification of PARP-1 affects interaction with chromatin and DNA to different extents. Here we describe a series of biochemical and biophysical techniques to quantify and dissect the different binding modes of PARP-1 with its various substrates. The techniques listed here allow for high throughput and quantitative measurements of the interaction of different PARP-1 constructs (inactive and automodified) with chromatin and DNA damage models.

Authors:
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  1. Children
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1418030
Resource Type:
Journal Article
Resource Relation:
Journal Name: Methods Mol. Biol.; Journal Volume: 1608; Journal Issue: 2017
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Chassé, Maggie H., Muthurajan, Uma M., Clark, Nicholas J., Kramer, Michael A., Chakravarthy, Srinivas, Irving, Thomas, Luger, Karolin, IIT), Colorado), and Amgen). Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin. United States: N. p., 2018. Web. doi:10.1007/978-1-4939-6993-7_16.
Chassé, Maggie H., Muthurajan, Uma M., Clark, Nicholas J., Kramer, Michael A., Chakravarthy, Srinivas, Irving, Thomas, Luger, Karolin, IIT), Colorado), & Amgen). Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin. United States. doi:10.1007/978-1-4939-6993-7_16.
Chassé, Maggie H., Muthurajan, Uma M., Clark, Nicholas J., Kramer, Michael A., Chakravarthy, Srinivas, Irving, Thomas, Luger, Karolin, IIT), Colorado), and Amgen). Thu . "Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin". United States. doi:10.1007/978-1-4939-6993-7_16.
@article{osti_1418030,
title = {Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin},
author = {Chassé, Maggie H. and Muthurajan, Uma M. and Clark, Nicholas J. and Kramer, Michael A. and Chakravarthy, Srinivas and Irving, Thomas and Luger, Karolin and IIT) and Colorado) and Amgen)},
abstractNote = {Poly (ADP-Ribose) Polymerase I (PARP-1) is a first responder to DNA damage and participates in the regulation of gene expression. The interaction of PARP-1 with chromatin and DNA is complex and involves at least two different modes of interaction. In its enzymatically inactive state, PARP-1 binds native chromatin with similar affinity as it binds free DNA ends. Automodification of PARP-1 affects interaction with chromatin and DNA to different extents. Here we describe a series of biochemical and biophysical techniques to quantify and dissect the different binding modes of PARP-1 with its various substrates. The techniques listed here allow for high throughput and quantitative measurements of the interaction of different PARP-1 constructs (inactive and automodified) with chromatin and DNA damage models.},
doi = {10.1007/978-1-4939-6993-7_16},
journal = {Methods Mol. Biol.},
number = 2017,
volume = 1608,
place = {United States},
year = {Thu Jan 18 00:00:00 EST 2018},
month = {Thu Jan 18 00:00:00 EST 2018}
}