Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.
Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.
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古菌DNA修复机制纳米生物马达：研究现状及应用潜力
DOI：
10.1186/2045-3701-4-32
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发表时间：
2014
影响因子：
7.5
通讯作者：
She Q
中科院分区：
文献类型：
--
作者：
Han W;Shen Y;She Q
纳米生物马达在细胞中发挥各种重要功能，并且它们也成为药物输送的潜在载体。这些蛋白质利用保守的 ATP 酶结构域将化学能转化为机械功和运动。一些古细菌核酸纳米生物马达，例如在 DNA 损伤修复过程中解旋双链 DNA 分子的 DNA 解旋酶，已经得到了详细的表征。 XPB、XPD 和 Hjm 是 SF2 家族解旋酶，每种解旋酶均采用两个 ATPase 结构域进行 ATP 结合和水解，以驱动 DNA 解旋。它们还携带用于底物结合和调节的额外特定结构域。另一种解旋酶 HerA 形成六聚环，可在双链 DNA 断裂的末端处理中充当 DNA 泵酶。所有这些纳米生物马达的共同点是它们含有采用 RecA 折叠结构的 ATPase 结构域。这种结构是 RecA/RadA 家族蛋白的特征，并且已被详细研究。在这里，我们回顾了这些古菌核酸生物马达的结构分析，以及 ATP 结合和水解如何促进驱动机械运动的构象变化的分子机制。讨论了古细菌纳米生物马达在药物输送中的应用潜力。
Nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. These proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Several archaeal nucleic acid nanobiomotors, such as DNA helicases that unwind double-stranded DNA molecules during DNA damage repair, have been characterized in details. XPB, XPD and Hjm are SF2 family helicases, each of which employs two ATPase domains for ATP binding and hydrolysis to drive DNA unwinding. They also carry additional specific domains for substrate binding and regulation. Another helicase, HerA, forms a hexameric ring that may act as a DNA-pumping enzyme at the end processing of double-stranded DNA breaks. Common for all these nanobiomotors is that they contain ATPase domain that adopts RecA fold structure. This structure is characteristic for RecA/RadA family proteins and has been studied in great details. Here we review the structural analyses of these archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion. The application potential of archaeal nanobiomotors in drug delivery has been discussed.
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