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首页> 外文期刊>Molecular and Cellular Biology >Quaternary Structure of ATR and Effects of ATRIP and Replication Protein A on Its DNA Binding and Kinase Activities
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Quaternary Structure of ATR and Effects of ATRIP and Replication Protein A on Its DNA Binding and Kinase Activities

机译：ATR的四级结构以及ATRIP和复制蛋白A对其DNA结合和激酶活性的影响

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摘要

ATR is an essential protein that functions as a damage sensor and a proximal kinase in the DNA damage checkpoint response in mammalian cells. It is a member of the phosphoinositide 3-kinase-like kinase (PIKK) family, which includes ATM, ATR, and DNA-dependent protein kinase. Recently, it was found that ATM is an oligomeric protein that is converted to an active monomeric form by phosphorylation in trans upon DNA damage, and this raised the possibility that other members of the PIKK family may be regulated in a similar manner. Here we show that ATR is a monomeric protein associated with a smaller protein called ATRIP with moderate affinity. The ATR protein by itself or in the form of the ATR-ATRIP heterodimer binds to naked or replication protein A (RPA)-covered DNAs with comparable affinities. However, the phosphorylation of RPA by ATR is dependent on single-stranded DNA and is stimulated by ATRIP. These findings suggest that the regulation and mechanism of action of ATR are fundamentally different from those of the other PIKK proteins.
机译：ATR是一种必需蛋白，在哺乳动物细胞的DNA损伤检查点反应中，它起损伤传感器和近端激酶的作用。它是磷酸肌醇3激酶样激酶（PIKK）家族的成员，该家族包括ATM，ATR和DNA依赖性蛋白激酶。最近发现，ATM是一种寡聚蛋白，在DNA损伤后通过 trans 的磷酸化作用转变为活性单体形式，这增加了PIKK家族其他成员可能受到调控的可能性。类似的方式。在这里，我们显示ATR是一种单体蛋白，与一种称为ATRIP的较小蛋白具有中等亲和力。 ATR蛋白本身或以ATR-ATRIP异二聚体形式与裸露或复制蛋白A（RPA）覆盖的DNA结合，具有相似的亲和力。但是，ATR使RPA磷酸化取决于单链DNA，并受ATRIP刺激。这些发现表明，ATR的调节和作用机理与其他PIKK蛋白完全不同。

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