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首页> 外文期刊>Nucleic Acids Research >Kinetic analysis of the nucleic acid chaperone activity of the Hepatitis C virus core protein
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Kinetic analysis of the nucleic acid chaperone activity of the Hepatitis C virus core protein

机译：丙型肝炎病毒核心蛋白的核酸伴侣活性的动力学分析

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摘要

The multifunctional HCV core protein consists of a hydrophilic RNA interacting D1 domain and a hydrophobic D2 domain interacting with membranes and lipid droplets. The core D1 domain was found to possess nucleic acid annealing and strand transfer properties. To further understand these chaperone properties, we investigated how the D1 domain and two peptides encompassing the D1 basic clusters chaperoned the annealing of complementary canonical nucleic acids that correspond to the DNA sequences of the HIV-1 transactivation response element TAR and its complementary cTAR. The core peptides were found to augment cTAR-dTAR annealing kinetics by at least three orders of magnitude. The annealing rate was not affected by modifications of the dTAR loop but was strongly reduced by stabilization of the cTAR stem ends, suggesting that the core-directed annealing reaction is initiated through the terminal bases of cTAR and dTAR. Two kinetic pathways were identified with a fast pre-equilibrium intermediate that then slowly converts into the final extended duplex. The fast and slow pathways differed by the number of base pairs, which should be melted to nucleate the intermediates. The three peptides operate similarly, confirming that the core chaperone properties are mostly supported by its basic clusters.
机译：多功能HCV核心蛋白由与D1结构域相互作用的亲水RNA和与膜和脂质液滴相互作用的疏水D2结构域组成。发现核心D1结构域具有核酸退火和链转移性质。为了进一步了解这些分子伴侣的特性，我们研究了D1结构域和两个包含D1基本簇的肽如何陪伴与HIV-1反式激活反应元件TAR及其互补cTAR的DNA序列相对应的互补经典核酸的退火。发现核心肽可将cTAR-dTAR退火动力学提高至少三个数量级。退火速率不受dTAR环修饰的影响，但由于cTAR茎端的稳定作用而大大降低，这表明核心导向的退火反应是通过cTAR和dTAR的末端碱基引发的。用快速的平衡前中间体鉴定了两个动力学途径，然后该中间体缓慢转化为最终的延伸双链体。快路径和慢路径的碱基对数量不同，应将其融化以使中间体成核。这三种肽的作用类似，这证实了核心分子伴侣的特性大部分受其基本簇支持。

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