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The interaction of p53 with 3'-terminal mismatched DNA.

机译：P53与3'-末端错配DNA的相互作用。

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摘要

The diversity of p53 functions involves its interaction with sequence-specific, non-sequence-specific and various damaged sites in DNA. The preferential excision of misincorporated over correct nucleotides by the 3'-->5' exonuclease activity of p53 provides a molecular basis for p53 involvement in the correction of the DNA replication errors. However, p53 exhibits variations in its comparative efficiency to excise different 3'-terminal mismatched nucleotides. To determine the importance of the binding capacity of the protein to various 3'-terminal damaged sites, we have examined the interaction of p53 with linear dsDNAs containing various 3'-terminal mismatches by employing a gel retardation assay. The data demonstrate the intrinsic 3'-terminal mismatched DNA binding capacity of p53. Since p53 binds directly to various 3'-terminal purine:pyrimidine and purine:purine mispairs to an equal extent, it can be considered a general 3'-mismatched DNA binding protein. Apparently, 3'-terminal mismatched bases are structural elements to which p53 can bind, that extends the spectrum of damage sites to which p53 may respond. The formation of the p53-mismatched DNA complex is independent of the sequence context. Thus, the dissimilarities in mispair excision efficiency are probably due to an inherent property of the p53 in the excision of 3'-mismatched nucleotides by a bound protein. The results establish a framework for understanding the mechanism of cooperative interaction between p53 and exonucleasedeficient DNA polymerase (e.g., HIV-1 RT). Within the context of error-correction events, p53 by recognition and excision of 3'-mismatched nucleotides, may be involved in DNA repair, thus increasing the accuracy of DNA synthesis by DNA polymerases.
机译：P53功能的多样性涉及其与DNA中序列特异性，非序列特异性和各种受损部位的相互作用。 P53的3' - > 5'外切核酸酶活性对正确的核苷酸的优先切除对正确的核苷酸的优先切除P53的分子基础是P53参与DNA复制误差的校正。然而，P53对其比较效率的变化进行了消除不同的3'-末端不匹配的核苷酸。为了确定蛋白质的结合能力对各种3'-末端受损的位点的重要性，我们通过采用凝胶延迟测定检查了P53与含有各种3'-末端不匹配的线性DSDNA的相互作用。数据证明了P53的内在3'-末端不匹配的DNA结合能力。由于P53直接与各种3'-末端嘌呤结合：嘧啶和嘌呤：嘌呤的错误分布在相等程度上，它可以被认为是一般的3'不匹配的DNA结合蛋白。显然，3'-末端不匹配的碱是P53可以结合的结构元素，其延伸了P53可以响应的损伤部位的光谱。 P53 - 失配DNA复合物的形成与序列背景无关。因此，错误切除效率的异化可能是由于P53在切除3'不匹配的核苷酸中通过结合蛋白质的固有性质。结果建立了理解P53与外切核DNA聚合酶（例如，HIV-1 RT）之间的协同相互作用机制的框架。在纠错事件的背景下，P53通过识别和切除3'不匹配的核苷酸，可以参与DNA修复，从而提高DNA聚合酶的DNA合成的准确性。

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  • 来源
    《Cell cycle》 |2010年第7期|共10页
  • 作者

    Bakhanashvili M; Rahav G;

  • 作者单位

    Infectious Diseases Unit Sheba Medical Center Tel Hashomer and The Mina and Everard Goodman Faculty of Life Sciences Bar-Ilan University Ramat-Gan Israel.;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 细胞生物学;
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