Specific Binding of Poly(ADP-ribose) Polymerase-1 to Cruciform Hairpins

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....

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Bibliographic Details
Published in:Journal of molecular biology 2005-05, Vol.348 (3), p.609-615
Main Authors: Potaman, Vladimir N., Shlyakhtenko, Luda S., Oussatcheva, Elena A., Lyubchenko, Yuri L., Soldatenkov, Viatcheslav A.
Format: Article
Language:English
Subjects:
cruciform hairpin
DNA - chemistry
DNA - metabolism
DNA Footprinting
DNA-binding
footprint
Gene Expression Regulation
Humans
Microscopy, Atomic Force
Nucleic Acid Conformation
PARP-1
Poly (ADP-Ribose) Polymerase-1
Poly(ADP-ribose) Polymerases - genetics
Poly(ADP-ribose) Polymerases - metabolism
Promoter Regions, Genetic
Protein Binding
transcriptional regulation
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2005.03.010