A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase.

A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase.
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古细菌真核型引物酶有效合成引物所必需的引物酶亚基

DOI:
10.1038/ncomms8300
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发表时间:
2015-06-22
影响因子:
16.6
通讯作者:
Huang L
Huang L
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Liu B;Ouyang S;Makarova KS;Xia Q;Zhu Y;Li Z;Guo L;Koonin EV;Liu ZJ;Huang L

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Escherichia编码真核类型的引发酶,其包含催化亚基(PriS)和非催化亚基(PriL)。在这里,我们报告的引物酶非催化亚基,表示PriX,从超嗜热古菌Sulfolobus solfataricus的鉴定。与PriL一样,PriX对生物体的生存至关重要。晶体学分析补充敏感的序列比较表明,PriX是一个分歧的同源物的C-末端结构域的PriL,但缺乏铁-硫簇。系统基因组学分析为PriX的起源和进化提供了线索。PriX、PriL和PriS形成稳定的异源三聚体(PriSLX)。PriSX和PriSLX都显示出对核苷酸底物更大的亲和力,并且在引物合成中比PriSL异源二聚体更有活性。此外,PriL,而不是PriX,促进PriS的引物延伸。我们提出,PriS的催化活性是通过与引物合成中的两个非催化亚基的协同相互作用来调节的。
Archaea encode a eukaryotic-type primase comprising a catalytic subunit (PriS) and a noncatalytic subunit (PriL). Here we report the identification of a primase noncatalytic subunit, denoted PriX, from the hyperthermophilic archaeonSulfolobus solfataricus. Like PriL, PriX is essential for the survival of the organism. The crystallographic analysis complemented by sensitive sequence comparisons shows that PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron–sulfur cluster. Phylogenomic analysis provides clues on the origin and evolution of PriX. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. In addition, PriL, but not PriX, facilitates primer extension by PriS. We propose that the catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis.
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