Rev1 employs a novel mechanism of DNA synthesis using a protein template
Rev1 employs a novel mechanism of DNA synthesis using a protein template
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DOI：
10.1126/science.1116336
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发表时间：
2005-09-30
期刊：
影响因子：
56.9
通讯作者：
Aggarwal, AK
中科院分区：
文献类型：
--
作者：
Nair, DT;Johnson, RE;Aggarwal, AK
Rev 1 DNA聚合酶高度特异性地用于C相对模板G的掺入。我们在此展示了与模板G和引入的2 '-脱氧胞苷5'-三磷酸（dCTP）结合的酵母Rev 1的晶体结构;这揭示了聚合酶本身决定了引入的核苷酸的身份以及模板碱基的身份。模板G和传入dCTP彼此不配对。相反，模板G从DNA螺旋中被驱逐，它与Rev 1的一段形成最佳氢键。此外，与其他DNA聚合酶不同，引入的dCTP与精氨酸而不是模板碱基配对，这确保了dCTP在其他引入的核苷酸上的掺入。这种机制提供了一个优雅的手段，促进熟练和无误的合成，通过N-2-加合鸟嘌呤，阻碍复制。
The Rev1 DNA polymerase is highly specialized for the incorporation of C opposite template G. We present here the crystal structure of yeast Rev1 bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP); which reveals that the polymerase itself dictates the identity of the incoming nucleotide, as well as the identity of the templating base. Template G and incoming dCTP do not pair with each other. Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating base, which ensures the incorporation of dCTP over other incoming nucleotides. This mechanism provides an elegant means for promoting proficient and error-free synthesis through N-2-adducted guanines that obstruct replication.