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CRYSTAL STRUCTURE OF THE PLANT TRANSCRIPTION FACTOR STWHY1 COMPLEXED WITH DNA

CRYSTAL STRUCTURE OF THE PLANT TRANSCRIPTION FACTOR STWHY1 COMPLEXED WITH DNA
植物转录因子 STWHY1 与 DNA 复合的晶体结构
批准号:
7358909
负责人:
JURGEN SYGUSCH
金额:
$0.31万
依托单位国家:
美国
项目类别:
财政年份:
2006
资助国家:
美国
项目状态:
已结题
起止时间:
2006-07-01 至 2007-06-30

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中文摘要
翻译
该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者(PI)可能从另一个NIH来源获得主要资金,因此可以在其他CRISP条目中表示。所列机构为中心机构,不一定为研究者机构。植物对病原体的防御反应主要依赖于使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是最好的特征。它被称为StWhy 1(Solanum tuberosum Whirly 1)的转录激活因子激活,该转录激活因子识别单链DNA。StWhy 1在植物界普遍存在,但与其他界中的任何其他蛋白质都不相关。我们解决了StWhy 1的未络合形式的晶体结构。StWhy 1的结构分析表明,该蛋白质以一种新的方式结合DNA,但结合机制尚未被表征。因此,我们建议解决一个StWhy 1/DNA复合物的结构,以表征蛋白质与其同源DNA元件的结合。已经获得了蛋白质/DNA复合物的晶体。他们在我们自己的X射线发生器中将其转换为7A。高通量光束线的使用将使我们能够获得高衍射图案,并允许我们解决蛋白质-DNA复合物的结构。这将使我们深入了解StWhy 1与DNA结合的机制以及它的转录激活。
英文摘要
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.
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