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首页> 外文期刊>Biochemistry >Poly(ADP-ribose)Polymerase-1 Dimerizes at a 5' Recessed DNA End in Vitro:A Fluorescence Study
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Poly(ADP-ribose)Polymerase-1 Dimerizes at a 5' Recessed DNA End in Vitro:A Fluorescence Study

机译：聚（ADP-核糖）聚合物1在体外5'凹入的DNA末端二聚：荧光研究

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Activation of poly(ADP-ribose)polymerase-1(PARP-1)is an immediate cellular reaction to DNA strand breakage as induced by alklating agents,ionizing radiation,or oxidants.The resulting formation of protein-bound poly(ADP-ribose)facilitates survival of proliferating cells under conditions of DNA damage probably via its contribution to DNA base excision repair.In this study,we investigated the association of the amino-terminal DNA base excision repair.In this study,we investigated the association of the amino-terminal DNA binding domain of human PARP-1(hPARP-1 DBD) with a 5' recessed oligonucleottide mimicking a telomeric DNA end.We used the fluorescence of the Trp residues naturally occurring inthe zinc finger domain of hPARP-1 DBD.Flluorescence intensity and fluorescence anisotropy measurements consistently show that the binding stoichiometry is two proteins per DNA molecule.hPARP-1 was found to bind the 5' recessed DNA end with a binding constnat of approx10~14 M~-2 if a cooperative binding model i sasssumed.These results indicate that hPARP-1 DBD is asymmetrically positioned at the junction between the double-stranded and the single-stranded telomeric repeat.The largest contribution to the stability of the complex is given by nonionic interactions.Moreover,time-resolved fluorescence measurements are in line with the involvement of one Trp residue in the stacking interaction fluorescnece measurements are in line with the involvement of one Trp residue in the stacking interaction with DNA bases.Taken together,our data open new perspectives for interpretatio of the selective binding of hPARP-1 to the junction between double- and single-stranded DNA.
机译：聚（ADP-核糖）聚合酶-1（PARP-1）的激活是由链烷剂，电离辐射或氧化剂诱导的DNA链断裂的立即细胞反应。形成的蛋白质结合聚（ADP-核糖）形成可能是通过促进DNA碱基切除修复来促进增殖细胞在DNA损伤条件下的存活。在这项研究中，我们研究了氨基末端DNA碱基切除修复的关联。人PARP-1（hPARP-1 DBD）的末端DNA结合结构域具有一个5'凹陷的寡核苷酸，模仿端粒DNA末端。我们使用了hPARP-1 DBD锌指结构域中天然存在的Trp残基的荧光。荧光各向异性测量结果一致地表明，结合化学计量是每个DNA分子两个蛋白质.hPARP-1被发现结合5'凹入的DNA末端，结合位点大约为10〜14 M〜-2（如果有一个合作伙伴）这些结果表明，hPARP-1 DBD不对称地位于双链和单链端粒重复序列之间的交界处。非离子相互作用对复合物的稳定性贡献最大。分辨的荧光测量结果符合一个Trp残基参与堆叠相互作用的过程荧光测量结果符合一个Trp残基参与与DNA碱基堆叠相互作用的过程。在一起，我们的数据为解释该化合物打开了新的前景。 hPARP-1与双链和单链DNA之间的连接的选择性结合。

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