TY - JOUR
T1 - 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
AU - Kim, In Kwon
AU - Stegeman, Roderick A.
AU - Brosey, Chris A.
AU - Ellenberger, Tom
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2015/2/6
Y1 - 2015/2/6
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.
UR - http://www.scopus.com/inward/record.url?scp=84922347288&partnerID=8YFLogxK
U2 - 10.1074/jbc.M114.624718
DO - 10.1074/jbc.M114.624718
M3 - Article
C2 - 25477519
AN - SCOPUS:84922347288
VL - 290
SP - 3775
EP - 3783
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 6
ER -