首页> 外文期刊>Nucleic Acids Research >DNA-BINDING PROPERTIES OF ARABIDOPSIS MADS DOMAIN HOMEOTIC PROTEINS APETALA1, APETALA3, PISTILLATA AND AGAMOUS
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DNA-BINDING PROPERTIES OF ARABIDOPSIS MADS DOMAIN HOMEOTIC PROTEINS APETALA1, APETALA3, PISTILLATA AND AGAMOUS

机译:拟南芥病菌域同源蛋白APETALA1,APETALA3,雌蕊和拟南芥的DNA结合特性

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The MADS domain proteins APETALA1 (AP1), APETALA3 (AP3), PISTILLATA (PI), and AGAMOUS (AG) specify the identity of Arabidopsis floral organs, AP1 and AG homocomplexes and AP3-PI heterocomplexes bind to CArG-box sequences, The DNA-binding properties of these complexes were investigated. We find that AP1, AG and AP3-PI are all capable of recognizing the same DNA-binding sites, although with somewhat different affinities, In addition, the three complexes induce similar conformational changes on a CArG-box sequence. Phasing analysis reveals that the induced distortion is DNA bending, oriented toward the minor groove. The molecular dissection of AP1, AP3, PI and AG indicates that the boundaries of the dimerization domains of these proteins vary, The regions required to form a DNA-binding complex include, in addition to the MADS box, the entire L region (which follows the MADS box) and the first putative amphipathic helix of the K box in the case of AP3-PI, while for AP1 and AG only a part of the L region is needed. The similarity of the DNA-binding properties of AP1, AP3-PI and AG is discussed with regard to the biological specificity that these proteins exhibit.
机译:MADS域蛋白APETALA1(AP1),APETALA3(AP3),PISTILLATA(PI)和AGAMOUS(AG)指定了拟南芥花器官,AP1和AG同质复合物以及AP3-PI异源复合物与CArG-box序列结合的身份研究了这些复合物的结合特性。我们发现,AP1,AG和AP3-PI都能够识别相同的DNA结合位点,尽管亲和性略有不同。此外,这三种复合物在CArG-box序列上诱导相似的构象变化。分阶段分析表明,诱发的扭曲是DNA弯曲,朝向小沟。 AP1,AP3,PI和AG的分子解剖表明,这些蛋白质的二聚化结构域的边界是变化的。形成DNA结合复合物所需的区域除了MADS框外,还包括整个L区域(以下是对于AP3-PI,则为MADS框)和K框的第一个假定的两亲螺旋,而对于AP1和AG,仅需要L区的一部分。关于这些蛋白表现出的生物学特异性,讨论了AP1,AP3-PI和AG的DNA结合特性的相似性。

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