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首页> 外文期刊>Biochemistry >Structures of the Catalytic Domain of Bacterial Primase DnaG in Complexes with DNA Provide Insight into Key Priming Events
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Structures of the Catalytic Domain of Bacterial Primase DnaG in Complexes with DNA Provide Insight into Key Priming Events

机译:用DNA复合物中细菌预碱基DNAG的催化结构域的结构提供了对关键引发事件的洞察力

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摘要

Bacterial primase DnaG is an essential nucleic acid polymerase that generates primers for replication of chromosomal DNA. The mechanism of DnaG remains unclear due to the paucity of structural information on DnaG in complexes with other replisome components. Here we report the first crystal structures of noncovalent DnaG–DNA complexes, obtained with the RNA polymerase domain of Mycobacterium tuberculosis DnaG and various DNA ligands. One structure, obtained with ds DNA, reveals interactions with DnaG as it slides on ds DNA and suggests how DnaG binds template for primer synthesis. In another structure, DNA in the active site of DnaG mimics the primer, providing insight into mechanisms for the nucleotide transfer and DNA translocation. In conjunction with the recent cryo-EM structure of the bacteriophage T7 replisome, this study yields a model for primer elongation and hand-off to DNA polymerase.
机译:细菌预级酶DNAG是一种基本核酸聚合酶,用于产生用于复制染色体DNA的引物。 由于与其他重复组分的复合物中的DNAG的结构信息缺乏,DNAG的机制仍然不明确。 在这里,我们报告了使用C结核分枝杆菌的RNA聚合结构域和各种DNA配体获得的非共价DNAG-DNA复合物的第一晶体结构。 用DS DNA获得一种结构,揭示了与DNAG的相互作用,因为它在DS DNA上滑动并表明DNAG如何结合引物合成的模板。 在另一种结构中,DNAG活性位点中的DNA模仿底漆,从而深入了解核苷酸转移和DNA易位的机制。 结合最近的噬菌体T7替换物的Cryo-EM结构,该研究产生了底漆伸长和递送至DNA聚合酶的模型。

著录项

  • 来源
    《Biochemistry》 |2018年第14期|共10页
  • 作者单位

    Department of Pharmaceutical Sciences College of Pharmacy University of Kentucky Lexington Kentucky 40536 United States;

    Department of Chemistry and Biochemistry University of California San Diego La Jolla California 92093 United States;

    Department of Pharmaceutical Sciences College of Pharmacy University of Kentucky Lexington Kentucky 40536 United States;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

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