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Reexamining the DNA target selectivity of Scalloped

机译：重新检查扇贝的DNA靶标选择性

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摘要

Selector proteins are transcription factors that coordinate the formation and identity of organs and appendages. The proper formation of these tissues requires the selector proteins to regulate the expression of a large set of genes. Many selector proteins are involved in regulating multiple developmental processes, yet it is not completely clear how they are able to activate different sets of genes in a tissue-specific manner. An association with cofactors is thought to be one method by which enhancer selectivity is achieved. During wing development the selector protein Scalloped (SD) interacts with the cofactor Vestigial (VG). This interaction leads to the activation of a specific set of downstream wing genes. Herein, data are presented indicating that the switch in binding selectivity is likely achieved by VG altering the general affinity that the SD protein has for DNA. The decreased affinity for DNA is compensated for by the fact that the VG protein forms a complex containing two SD proteins. These two properties ensure that the SD–VG complex is able to bind only to enhancers that have two consecutive binding sites. Furthermore, data are presented that indicate that the function of the two terminal domains of the VG protein is not restricted to activating transcription and promoting the recruitment of two SD proteins.
机译：选择蛋白是协调器官和附件的形成和身份的转录因子。这些组织的正确形成需要选择蛋白来调节大量基因的表达。许多选择蛋白参与调节多个发育过程，但尚不清楚它们如何以组织特异性方式激活不同的基因集。与辅因子的结合被认为是实现增强子选择性的一种方法。在机翼发育过程中，扇形选择蛋白（SD）与辅因子前庭（VG）相互作用。这种相互作用导致一组特定的下游侧翼基因的激活。在本文中，提供了数据，表明通过VG改变SD蛋白对DNA的一般亲和力可能实现了结合选择性的转变。 VG蛋白形成包含两个SD蛋白的复合物这一事实可以弥补对DNA亲和力下降的补偿。这两个特性确保SD-VG复合物仅能结合具有两个连续结合位点的增强子。此外，提供的数据表明VG蛋白的两个末端结构域的功能不限于激活转录和促进两个SD蛋白的募集。

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