CRYSTAL STRUCTURE OF THE PLANT TRANSCRIPTION FACTOR STWHY1 COMPLEXED WITH DNA

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 植物对病原体的防御反应主要依赖于利用预先存在的物理屏障和诱导防御，这需要大量转录防御基因。在反应防御过程中诱导的基因中，PR-10a的特性最好。它是由一种名为StWhy1(Solanum Tuberosum Whirly 1)的转录激活剂激活的，它识别单链DNA。StWhy1在植物界中普遍存在，但与其他物种中的任何其他蛋白质无关。我们解决了未络合形式的StWhy1的晶体结构。StWhy1的结构分析表明，该蛋白以一种新的方式与DNA结合，但结合机制尚未确定。因此，我们建议解决StWhy1/DNA复合体的结构，以表征蛋白质与其同源DNA元件的结合。蛋白质/DNA复合体的晶体已经获得。在我们自己的X射线发生器中，它们的衍射率为7A。高通量光束线的使用将使我们能够获得高的衍射图，并使我们能够解决蛋白质-DNA的复杂结构。这将使我们深入了解StWhy1与DNA结合的机制以及它对转录的激活。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The plant defense response to pathogens relies primarily on the use of pre-existing physical barriers and inducible defenses, which require massive transcription of defense genes. Among the genes induced during the response defense, PR-10a is the best characterized. It is activated by a transcription activator termed StWhy1 (Solanum tuberosum Whirly 1) which recognize single-strand DNA. StWhy1 is ubiquitous among plants kingdom but is not related to any other protein in other kingdoms. The crystal structure of the uncomplexed form of StWhy1 was solved by us. Structural analyses of StWhy1 have suggested that the protein binds DNA in a novel way but the binding mechanism has not been characterized yet. We therefore propose to solve the structure of a StWhy1/DNA complex to characterize the binding of the protein to its cognate DNA element. Crystals of the protein/DNA complex have already been obtained. They diffract to 7A in our own X-rays generator. The use of high-flux beamline would enable us to obtain high diffraction pattern and permit us to solve the protein-DNA complex structure. This would give us insight into the mechanism of DNA binding by StWhy1 as well as its activation of transcription.