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Contribution of Individual Amino Acids to the RNA Binding Activity of the Wilms’ Tumor Suppressor Protein WT1

机译：单个氨基酸对威尔姆斯肿瘤抑制蛋白WT1的RNA结合活性的贡献。

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摘要

In addition to binding to DNA, the zinc finger protein WT1 can also bind specifically to RNA. To determine the role of individual zinc fingers of the protein in this RNA binding activity, deletion and substitution mutants of the WT1 zinc finger domain were constructed. The effects of the various mutations on the binding of WT1 to the RNA aptamers RNA22 and RNA38 were determined using a quantitative equilibrium binding assay. The results indicate that zinc fingers 2 and 3 of WT1 are essential for the binding of the protein to the RNA aptamers. For both of these fingers, the arginine residue immediately preceding the α-helix makes a significant contribution to RNA binding. For zinc finger 2, a second arginine residue within the α-helix is also critical for RNA binding, while several α-helical residues in zinc finger 3 contribute to the overall affinity of WT1 for RNA. Investigating the effects of the same point mutations on DNA binding indicates that there are similarities and differences in the contributions of zinc fingers 2 and 3 to the DNA and RNA binding activities of WT1.
机译：除与DNA结合外，锌指蛋白WT1还可以与RNA特异性结合。为了确定蛋白质的各个锌指在该RNA结合活性中的作用，构建了WT1锌指结构域的缺失和取代突变体。使用定量平衡结合测定法确定了各种突变对WT1与RNA适体RNA22和RNA38结合的影响。结果表明WT1的锌指2和3对于蛋白质与RNA适体的结合至关重要。对于这两个手指，紧接在α-螺旋之前的精氨酸残基对RNA结合起了重要作用。对于锌指2，α螺旋中的第二个精氨酸残基对于RNA结合也很关键，而锌指3中的几个α螺旋残基有助于WT1对RNA的整体亲和力。研究相同点突变对DNA结合的影响表明，锌指2和3对WT1的DNA和RNA结合活性的贡献存在相似性和差异性。

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  • 来源
    《Biochemistry》 |2009年第1期|p.148-155|共8页
  • 作者

    Tristen C. Weiss and Paul J. Romaniuk;

  • 作者单位

    Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, Victoria, British Columbia V8W 3P6, Canada;

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