TY - JOUR
T1 - Specific binding of poly(ADP-ribose) polymerase-1 to cruciform hairpins
AU - Potaman, Vladimir N.
AU - Shlyakhtenko, Luda S.
AU - Oussatcheva, Elena A.
AU - Lyubchenko, Yuri L.
AU - Soldatenkov, Viatcheslav A.
N1 - Funding Information:
We thank Alexander Gamero for construction of plasmids pAG2 and pAG3 and help in heteroduplex purification, Irina Lonskaya for the PARP-1 purity assay and Richard R. Sinden for comments on the manuscript. This work was supported by National Institutes of Health grants CA74175 and GM62235 and Texas A & M University System Health Science Center.
PY - 2005/5/6
Y1 - 2005/5/6
N2 - 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.
AB - 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.
KW - Cruciform hairpin
KW - DNA-binding
KW - Footprint
KW - PARP-1
KW - Transcriptional regulation
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U2 - 10.1016/j.jmb.2005.03.010
DO - 10.1016/j.jmb.2005.03.010
M3 - Article
C2 - 15826658
AN - SCOPUS:17144423943
SN - 0022-2836
VL - 348
SP - 609
EP - 615
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -