HIV-1 nucleocapsid proteins as molecular chaperones for tetramolecular antiparallel G-quadruplex formation.
HIV-1 nucleocapsid proteins as molecular chaperones for tetramolecular antiparallel G-quadruplex formation.
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DOI：
10.1021/ja409085j
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发表时间：
2013-12-11
影响因子：
15
通讯作者：
Sugiyama H
中科院分区：
文献类型：
--
作者：
Rajendran A;Endo M;Hidaka K;Tran PL;Mergny JL;Gorelick RJ;Sugiyama H
HIV-1核衣壳蛋白(NCP)促进核酸的重塑，折叠成热力学稳定的构象，因此被称为核酸伴侣蛋白。到目前为止，关于化学计量、NCP-NCP相互作用、G-四链构象上的伴侣活性等方面的研究还很少。我们报道了用DNA折纸对蛋白质降解中间体NCp15和成熟的NCp7进行直接和实时的分析。蛋白质颗粒主要以单体形式存在，在自由溶液中也观察到二聚体和多聚体的存在，并与四链结构结合。G-四链体的形成和解离事件被实时记录下来，类中间态也被可视化。我们期待这一开创性的研究将加深我们对HIV-1蛋白伴侣活性的理解，这将有助于基于G-四链的药物设计，也将有助于抗艾滋病药物的开发。
HIV-1 nucleocapsid proteins (NCps) facilitate remodeling of nucleic acids to fold thermodynamically stable conformations, and thus called nucleic acid chaperones. To date only little is known on the stoichiometry, NCp-NCp interactions, chaperone activity on G-quadruplex formation, and so on. We report here the direct and real-time analysis on such properties of proteolytic intermediate NCp15 and mature NCp7 using DNA origami. The protein particles were found to predominantly exist in monomeric form, while dimeric and multimeric forms were also observed both in free solution and bound to the quadruplex structure. The formation and the dissociation events of the G-quadruplexes were well documented in real-time and the intermediate-like states were also visualized. We anticipate that this pioneering study will strengthen our understanding on the chaperone activity of HIV-1 proteins which in turn will be helpful for the drug design based on G-quadruplex and also for the development of drugs against AIDS.
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