Pieler T, Guddat U, Oei S L, Erdmann V A
Nucleic Acids Res. 1986 Aug 11;14(15):6313-26. doi: 10.1093/nar/14.15.6313.
Xenopus laevis 5S rRNA isolated from 7S particles or transcribed in vitro is found to adopt two alternative conformations. These two conformers contain different structural elements within the major TF III A binding domain, which, when isolated as RNA fragments, still interact with the transcription factor. Chemical modification of easily accessible adenines in their N-1 position does not have any measurable effect on the binding of 5S rRNA to TF III A. These observations are in support of the idea that only a small amount of conserved sequence information is required for the binding of the transcription factor, whereas specific secondary structure features seem to be essential.
从7S颗粒中分离或体外转录得到的非洲爪蟾5S rRNA呈现出两种不同的构象。这两种构象体在主要的TF III A结合结构域内包含不同的结构元件，当作为RNA片段分离时，它们仍能与转录因子相互作用。对其N-1位置易于接近的腺嘌呤进行化学修饰，对5S rRNA与TF III A的结合没有任何可测量的影响。这些观察结果支持这样一种观点，即转录因子结合仅需要少量保守序列信息，而特定的二级结构特征似乎至关重要。
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