ATP serves as a nucleotide switch coupling the genome maturation and packaging motor complexes of a virus assembly machine.

ATP serves as a nucleotide switch coupling the genome maturation and packaging motor complexes of a virus assembly machine.
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ATP 充当连接基因组成熟和病毒组装机的包装运动复合体的核苷酸开关。

DOI:
10.1093/nar/gkaa205
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发表时间:
2020
影响因子:
14.9
通讯作者:
Catalano,CarlosE
Catalano,CarlosE
中科院分区:
生物学2区
文献类型:
--
作者:
Yang,Qin;Catalano,CarlosE

文献摘要

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从噬菌体到疱疹病毒,双链DNA病毒的组装是高度保守的。终止酶从连接的DNA底物中不断地切除和包装单体基因组。酶在稳定的成熟复合体和动态的马达复合体之间循环,前者在双链中引入位点特异性的切口,后者在ATP水解的推动下将DNA快速易位到原衣壳中。这些紧密耦合的反应由末端酶催化,末端酶组装成两个功能不同的核蛋白复合物;分别是成熟复合物和包装马达复合物。我们描述了核苷酸对病毒DNA上具有催化能力的成熟复合体组装的影响,它们对成熟复合体稳定性的影响以及它们向活性包装马达复合体过渡的要求。ATP在调节所有这些活动中起着重要作用,并可能作为“核苷酸开关”,在基因包装过程中介导两种复合物之间的转换。这些生物学过程在所有从串联DNA底物中包装单体基因组的dsDNA病毒中都有重现,核苷酸开关机制可能对病毒组装机制具有广泛的生物学意义。
The assembly of double-stranded DNA viruses, from phages to herpesviruses, is strongly conserved. Terminase enzymes processively excise and package monomeric genomes from a concatemeric DNA substrate. The enzymes cycle between a stable maturation complex that introduces site-specific nicks into the duplex and a dynamic motor complex that rapidly translocates DNA into a procapsid shell, fueled by ATP hydrolysis. These tightly coupled reactions are catalyzed by terminase assembled into two functionally distinct nucleoprotein complexes; thematuration complexand thepackaging motor complex, respectively. We describe the effects of nucleotides on the assembly of a catalytically competent maturation complex on viral DNA, their effect on maturation complex stability and their requirement for the transition to active packaging motor complex. ATP plays a major role in regulating all of these activities and may serve as a ‘nucleotide switch’ that mediates transitions between the two complexes during processive genome packaging. These biological processes are recapitulated in all of the dsDNA viruses that package monomeric genomes from concatemeric DNA substrates and the nucleotide switch mechanism may have broad biological implications with respect to virus assembly mechanisms.