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. 2005 May 6;348(3):609-15.
doi: 10.1016/j.jmb.2005.03.010.

Specific binding of poly(ADP-ribose) polymerase-1 to cruciform hairpins

Vladimir N Potaman  1 , Luda S Shlyakhtenko, Elena A Oussatcheva, Yuri L Lyubchenko, Viatcheslav A Soldatenkov
Affiliations

Specific binding of poly(ADP-ribose) polymerase-1 to cruciform hairpins

Vladimir N Potaman et al. J Mol Biol. .

Abstract

Poly(ADP-ribose) polymerase-1 (PARP-1) participates in DNA cleavage and rejoining-dependent reactions, such as DNA replication, recombination and repair. PARP-1 is also important in transcriptional regulation, although the determinants for its binding to undamaged genomic DNA have not been defined. Previously, we have shown by low-resolution mapping that PARP-1 may bind to the cruciform-forming regions of its own promoter. Here, using DNase I and nuclease P(1) footprinting and atomic force microscopy, we show that PARP-1 binds to stem/loop boundaries of cruciform hairpins. Cleavage of the cruciform by the junction resolvase T4 endonuclease VII is independent of PARP-1, which indicates that PARP-1 does not bind to the four-arm junctions of the cruciform. Thus, PARP-1 differs from other cruciform-binding proteins by binding to hairpin tips rather than to junctions. Furthermore, our data indicate that PARP-1 can interact with the gene regulatory sequences by binding to the promoter-localized cruciforms.

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