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首页> 外文期刊>Journal of Molecular Biology >Novel interaction of the bacterial-like DnaG primase with the MCM helicase in archaea
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Novel interaction of the bacterial-like DnaG primase with the MCM helicase in archaea

机译：细菌样DnaG引发酶与古细菌中MCM解旋酶的新型相互作用

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DNA priming and unwinding activities are coupled within bacterial primosome complexes to initiate synthesis on the lagging strand during DNA replication. Archaeal organisms contain conserved primase genes homologous to both the bacterial DnaG and archaeo-eukaryotic primase families. The inclusion of multiple DNA primases within a whole domain of organisms complicates the assignment of the metabolic roles of each. In support of a functional bacterial-like DnaG primase participating in archaeal DNA replication, we have detected an interaction of Sulfolobus solfataricus DnaG (SsoDnaG) with the replicative S. solfataricus minichromosome maintenance (SsoMCM) helicase on DNA. The interaction site has been mapped to the N-terminal tier of SsoMCM analogous to bacterial primosome complexes. Mutagenesis within the metal binding site of SsoDnaG verifies a functional homology with bacterial DnaG that perturbs priming activity and DNA binding. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged. Competition for binding DNA between SsoDnaG and SsoMCM can reduce the unwinding ability. Fluorescent gel shift experiments were used to quantify the binding of the ternary SsoMCM-DNA-SsoDnaG complex. This direct interaction of a bacterial-like primase with a eukaryotic-like helicase suggests that formation of a unique but homologous archaeal primosome complex is possible but may require other components to stimulate activities. Identification of this archaeal primosome complex broadly impacts evolutionary relationships of DNA replication.
机译：DNA引发和解链活性在细菌的原始体复合物中偶联，以在DNA复制过程中在落后链上启动合成。古细菌生物体包含与细菌DnaG和古生物真核酶家族均同源的保守的蛋白酶基因。在整个生物域中包含多个DNA引发酶会使每种生物的代谢作用分配变得复杂。为了支持参与古细菌DNA复制的功能性细菌样DnaG引发酶，我们检测到了Sulfolobus solfataricus DnaG（SsoDnaG）与DNA上的S. solfataricus minichromosome维持型（SsoMCM）解旋酶的相互作用。相互作用位点已映射到SsoMCM的N端层，类似于细菌的原核小体复合物。 SsoDnaG的金属结合位点内的诱变验证了与细菌DnaG的功能同源性，该功能性干扰了启动活性和DNA结合。 SsoDnaG与SsoMCM的复合物刺激SsoMCM的ATPase活性，但保持SsoDnaG的启动活性不变。 SsoDnaG与SsoMCM之间结合DNA的竞争会降低解链能力。荧光凝胶位移实验用于定量三元SsoMCM-DNA-SsoDnaG复合物的结合。细菌样启动酶与真核样解旋酶的这种直接相互作用表明可能形成独特但同源的古细菌初生体复合物，但可能需要其他成分来刺激活性。这种古细菌的原始体复合物的鉴定会广泛影响DNA复制的进化关系。

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