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首页> 外文期刊>Journal of Molecular Biology >Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function.
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Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function.

机译：人类免疫缺陷病毒1型核衣壳蛋白p7与模型RNA的结合特性：功能的结构决定子的阐明。

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摘要

HIV-1 nucleocapsid protein (NCp7) is a double zinc-fingered protein that has been traditionally implicated in viral RNA recognition and packaging, in addition to its tight association with genomic RNA and tRNA primer within the virion nucleocapsid. The availability of large quantities of viral or recombinant wild-type NCp7 and mutant p7 has made possible the assignment of the different roles that structural motifs within the protein play during RNA binding. At low ionic strength binding to the homopolymeric fluorescent RNA, poly(epsilonA), is electrostatically driven and four sodium ions are displaced. Arg7 in the flanking N-terminal region, Lys20 and Lys26 in the first zinc finger and one positively charged residue (attributed to Lys41) in the second zinc finger are involved in electrostatic contacts with RNA. The p7 zinc fingers do not function independently but concomitantly. The first zinc finger (both isolated or in the context of the full-length protein) has a more prominent electrostatic interaction than the second one. The second zinc finger dominates the non-electrostatic stabilization of the binding to RNA due to stacking of its Trp residue with nucleic acid bases. Mutations in the highly conserved retroviral Zn-coordinating residues (CCHC) to steroid hormone receptor (CCCC) or transcription factor (CCHH) metal cluster types do not affect RNA binding. In spite of the limited impact in RNA binding affinity in vitro or RNA packaging in vivo that such mutations or structural alterations impart, they impair or abolish virus infectivity. It is likely that such an effect stems from the involvement of NCp7 in crucial steps of the virus life cycle other than RNA binding. Copyright 1999 Academic Press.
机译：HIV-1核衣壳蛋白（NCp7）是双锌指蛋白，除与病毒体核衣壳中的基因组RNA和tRNA引物紧密结合外，传统上还涉及病毒RNA的识别和包装。大量病毒或重组野生型NCp7和突变体p7的可用性使人们可以确定蛋白质内部结构基序在RNA结合过程中发挥的不同作用。在低离子强度下，静电驱动与均聚荧光RNA结合的聚（εA），并置换四个钠离子。 N末端侧翼的Arg7，第一个锌指中的Lys20和Lys26和第二个锌指中的一个带正电的残基（归因于Lys41）与RNA静电接触。 p7锌指并非独立运行，而是同时运行。第一个锌指（无论是分离的还是在全长蛋白质的上下文中）都比第二个锌指具有更突出的静电相互作用。由于其Trp残基与核酸碱基堆积，第二个锌指支配了与RNA结合的非静电稳定作用。高度保守的逆转录病毒锌配位残基（CCHC）突变为类固醇激素受体（CCCC）或转录因子（CCHH）金属簇类型不会影响RNA结合。尽管此类突变或结构改变对体外RNA结合亲和力或体内RNA包装的影响有限，但它们削弱或消除了病毒的感染性。这种作用可能是由于NCp7参与了病毒生命周期的关键步骤而不是RNA结合。版权所有1999，学术出版社。

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