Binding kinetics and activity of human poly(ADP-ribose) polymerase-1 on oligo-deoxyribonucleotide substrates.
Binding kinetics and activity of human poly(ADP-ribose) polymerase-1 on oligo-deoxyribonucleotide substrates.
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DOI：
10.1002/jmr.962
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发表时间：
2009-11
影响因子：
2.7
通讯作者：
Uren, Aykut
中科院分区：
文献类型：
--
作者：
Jorgensen, Timothy J.;Chen, Kevin;Chasovskikh, Sergey;Roy, Rabindra;Dritschilo, Anatoly;Uren, Aykut
关键词：
Poly(ADP-ribose) polymerase-1 (PARP-1) is a mammalian enzyme that attaches long branching chains of ADP-ribose to specific nuclear proteins, including itself. Because its activity in vitro is dependent upon interaction with broken DNA, it has been postulated that PARP-1 plays an important role in DNA strand-break repair in vivo. The exact mechanism of binding to DNA and the structural determinants of binding remain to be defined, but regions of transition from single-stranded to double-strandedness may be important recognition sites. Here we employ surface plasmon resonance (SPR) to investigate this hypothesis. Oligodeoxynucleotide (ODN) substrates that mimic DNA with different degrees of single-strandedness were used for measurements of both PARP-1/DNA binding kinetics and PARP-1’s enzyme activities. We found that binding correlated with activity, but was unrelated to single-strandedness of the ODN. Instead, PARP-1 binding and activity were highest on ODNs that modeled a DNA double-strand break (DSB). These results provide support for PARP-1 recognizing and binding DSBs in a manner that is independent of single-stranded features, and demonstrate the usefulness of SPR for simultaneously investigating both PARP-1 binding and PARP-1 auto-poly(ADP-ribosyl)ation activities within the same in vitro system.
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影响因子：
8
作者：
Day, YSN;Baird, CL;Myszka, DG
通讯作者：
Myszka, DG
影响因子：
5.3
作者：
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DOI：
10.1016/0006-291x(90)92102-6
发表时间：
1990-03-16
影响因子：
3.1
作者：
SASTRY, SS;KUN, E
通讯作者：
KUN, E
影响因子：
14.9
作者：
El-Khamisy, SF;Masutani, M;Caldecott, KW
通讯作者：
Caldecott, KW