A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase

In Kwon Kim; Roderick A. Stegeman; Chris A. Brosey; Tom Ellenberger

doi:10.1074/jbc.M114.624718

A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase

In Kwon Kim, Roderick A. Stegeman, Chris A. Brosey, Tom Ellenberger

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

Background: The DNA repair scaffold XRCC1 binds to poly(ADP-ribose)ylated PARP1 at damaged chromatin. Results: XRCC1 preferentially binds to poly(ADP-ribose) chains longer than 7 ADP-ribose units in length. Conclusion: We identify specific determinants of XRCC1-PARP1 complex assembly, and disassembly by PARG. Significance: Our TR-FRET assay is useful for investigating turnover of posttranslational modifications and for identifying inhibitors by high-throughput screening.

Original language	English (US)
Pages (from-to)	3775-3783
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	290
Issue number	6
DOIs	https://doi.org/10.1074/jbc.M114.624718
State	Published - Feb 6 2015
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Kim, I. K., Stegeman, R. A., Brosey, C. A., & Ellenberger, T. (2015). A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase. Journal of Biological Chemistry, 290(6), 3775-3783. https://doi.org/10.1074/jbc.M114.624718

A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase. / Kim, In Kwon; Stegeman, Roderick A.; Brosey, Chris A. et al.
In: Journal of Biological Chemistry, Vol. 290, No. 6, 06.02.2015, p. 3775-3783.

Research output: Contribution to journal › Article › peer-review

Kim, IK, Stegeman, RA, Brosey, CA & Ellenberger, T 2015, 'A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase', Journal of Biological Chemistry, vol. 290, no. 6, pp. 3775-3783. https://doi.org/10.1074/jbc.M114.624718

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abstract = "Background: The DNA repair scaffold XRCC1 binds to poly(ADP-ribose)ylated PARP1 at damaged chromatin. Results: XRCC1 preferentially binds to poly(ADP-ribose) chains longer than 7 ADP-ribose units in length. Conclusion: We identify specific determinants of XRCC1-PARP1 complex assembly, and disassembly by PARG. Significance: Our TR-FRET assay is useful for investigating turnover of posttranslational modifications and for identifying inhibitors by high-throughput screening.",

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AU - Brosey, Chris A.

AU - Ellenberger, Tom

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N2 - Background: The DNA repair scaffold XRCC1 binds to poly(ADP-ribose)ylated PARP1 at damaged chromatin. Results: XRCC1 preferentially binds to poly(ADP-ribose) chains longer than 7 ADP-ribose units in length. Conclusion: We identify specific determinants of XRCC1-PARP1 complex assembly, and disassembly by PARG. Significance: Our TR-FRET assay is useful for investigating turnover of posttranslational modifications and for identifying inhibitors by high-throughput screening.

AB - Background: The DNA repair scaffold XRCC1 binds to poly(ADP-ribose)ylated PARP1 at damaged chromatin. Results: XRCC1 preferentially binds to poly(ADP-ribose) chains longer than 7 ADP-ribose units in length. Conclusion: We identify specific determinants of XRCC1-PARP1 complex assembly, and disassembly by PARG. Significance: Our TR-FRET assay is useful for investigating turnover of posttranslational modifications and for identifying inhibitors by high-throughput screening.

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A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase

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