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 journalArticlepeer-review

37 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 languageEnglish
Pages (from-to)3775-3783
Number of pages9
JournalJournal of Biological Chemistry
Volume290
Issue number6
DOIs
StatePublished - Feb 6 2015

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