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

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

Research output: Contribution to journalArticlepeer-review

59 Scopus citations


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 P1 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.

Original languageEnglish (US)
Pages (from-to)609-615
Number of pages7
JournalJournal of Molecular Biology
Issue number3
StatePublished - May 6 2005


  • Cruciform hairpin
  • DNA-binding
  • Footprint
  • PARP-1
  • Transcriptional regulation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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