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首页> 外文期刊>Journal of Molecular Biology >E-BOX VARIANTS DIRECT FORMATION OF DISTINCT COMPLEXES WITH THE BASIC HELIX-LOOP-HELIX PROTEIN ALF1
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E-BOX VARIANTS DIRECT FORMATION OF DISTINCT COMPLEXES WITH THE BASIC HELIX-LOOP-HELIX PROTEIN ALF1

机译：E-BOX变体直接与基本的HELIX-LOOP-HELIX蛋白质ALF1形成复合物

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摘要

The murine transcription factor ALF1 belongs to the class of basic helix-loop-helix proteins specific for the NCAGNTGN-version of the E-box. Binding of homodimeric ALF1 to variants of this motif was studied by a combination of binding site selection technology and DNA modification interference analysis. The results showed that substitutions at the non-conserved positions in the E-box sequence could cause profound alterations in the patterns of specific contacts at the protein-DNA interface. Thus, both the overall extent of the binding region and the backbone phosphate contact pattern differed markedly between closely related E-boxes with similar affinities for ALF1. The identity of the base at the inner N was an important determinant of contact pattern specification. The E-box variants differed in their ability to mediate ALF1 dependent transcriptional activation in vivo. We discuss the possibility that adaptability in basic helix-loop-helix protein-DNA interactions can result in complexes with different functional properties. [References: 48]
机译：鼠转录因子ALF1属于对E-box的NCAGNTGN版本具有特异性的基本螺旋-环-螺旋蛋白。通过结合位点选择技术和DNA修饰干扰分析的组合，研究了同型二聚体ALF1与该基序变体的结合。结果表明，在E-box序列中非保守位置的取代可能导致蛋白质-DNA界面上特定接触方式的深刻改变。因此，结合区域的总范围和主链磷酸酯接触模式在与ALF1具有相似亲和力的密切相关的E-box之间明显不同。内部N处的碱基身份是确定接触图案的重要因素。 E-box变体在体内介导ALF1依赖性转录激活的能力不同。我们讨论了基本螺旋-环-螺旋蛋白质-DNA相互作用中的适应性可能导致具有不同功能特性的复合物的可能性。 [参考：48]

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