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首页> 外文期刊>PLoS Pathogens >Full-length human cytomegalovirus terminase pUL89 adopts a two-domain structure specific for DNA packaging
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Full-length human cytomegalovirus terminase pUL89 adopts a two-domain structure specific for DNA packaging

机译：全长人巨细胞病毒终酶脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲剂

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摘要

A key step in replication of human cytomegalovirus (HCMV) in the host cell is the generation and packaging of unit-length genomes into preformed capsids. The enzymes involved in this process are the terminases. The HCMV terminase complex consists of two terminase subunits, the ATPase pUL56 and the nuclease pUL89. A potential third component pUL51 has been proposed. Even though the terminase subunit pUL89 has been shown to be essential for DNA packaging and interaction with pUL56, it is not known how pUL89 mechanistically achieves sequence-specific DNA binding and nicking. To identify essential domains and invariant amino acids vis-a-vis nuclease activity and DNA binding, alanine substitutions of predicted motifs were analyzed. The analyses indicated that aspartate 463 is an invariant amino acid for the nuclease activity, while argine 544 is an invariant aa for DNA binding. Structural analysis of recombinant protein using electron microscopy in conjunction with single particle analysis revealed a curvilinear monomer with two distinct domains connected by a thinner hinge-like region that agrees well with the predicted structure. These results allow us to model how the terminase subunit pUL89’s structure may mediate its function.
机译：在宿主细胞中复制人巨细胞病毒（HCMV）的关键步骤是单位长度基因组的产生和包装成预成型衣壳。参与该过程的酶是术语。 HCMV末端酶复合物由两个术语酶亚基，ATP酶脉冲脉冲柱和核酸酶组成。已经提出了潜在的第三组分脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲脉冲柱51。即使终止酶亚单位脉冲脉冲脉冲脉冲为必不可少的DNA包装和与脉冲脉冲的相互作用是必不可少的，其尚不知道普拉斯89如何机械地实现序列特异性DNA结合和切口。为了鉴定基本结构域和不变的氨基酸Vis-A-Vis核酸酶活性和DNA结合，分析了预测基序的丙氨酸取代。分析表明，天冬氨酸463是核酸酶活性的不变氨基酸，而律法544是用于DNA结合的不变AA。结合单颗粒分析使用电子显微镜的重组蛋白的结构分析揭示了一种具有两个不同畴的曲线单体，其通过与预测结构吻合良好的较薄铰链状区域。这些结果允许我们模拟终止酶亚单元脉冲脉冲89的结构如何介导其功能。

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