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Structural basis for RNA-silencing suppression by Tomato aspermy virus protein 2b

机译:番茄曲霉病毒蛋白2b抑制RNA沉默的结构基础

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The 2b proteins encoded by cucumovirus act as post-transcriptional gene silencing suppressors to counter host defence during infection. Here we report the crystal structure of Tomato aspermy virus 2b (TAV2b) protein bound to a 19 bp small interfering RNA (siRNA) duplex. TAV2b adopts an all a-helix structure and forms a homodimer to measure siRNA duplex in a length-preference mode. TAV2b has a pair of hook-like structures to recognize simultaneously two a-helical turns of A-form RNA duplex by fitting its a-helix backbone into two adjacent major grooves of siRNA duplex. The conserved p-stackings between tryptophan and the 50-terminal base of siRNA duplex from both ends enhance the recognition. TAV2b further oligomerizes to form a dimer of dimers through the conserved leucine-zipper-like motif at its amino-terminal a-helix. Biochemical experiments suggest that TAV2b might interfere with the post-transcriptional gene silencing pathway by directly binding to siRNA duplex.
机译:黄瓜花叶病毒编码的2b蛋白充当转录后基因沉默抑制剂,以抵抗感染期间的宿主防御。在这里,我们报告与19 bp小干扰RNA(siRNA)双链体结合的番茄曲霉病毒2b(TAV2b)蛋白的晶体结构。 TAV2b采用全a螺旋结构,并形成同源二聚体,以长度优先模式测量siRNA双链体。 TAV2b具有一对钩状结构,可通过将其a螺旋骨架安装到siRNA双链体的两个相邻主要凹槽中来同时识别A型RNA双链体的两个a螺旋圈。色氨酸与siRNA双链体两端的50末端碱基之间的保守p堆积增强了识别能力。 TAV2b通过其氨基末端a螺旋上保守的亮氨酸拉链样基序进一步低聚形成二聚体的二聚体。生化实验表明,TAV2b可能通过直接结合siRNA双链体而干扰转录后基因沉默途径。

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