STRUCTURE DETERMINATION OF THE CHD1 DNA-BINDING DOMAIN

CHD1 DNA 结合域的结构测定

• 批准号: 8363383
• 负责人: GREGORY DEAN BOWMAN
• 金额: $ 0.31万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363383
• 关键词: Binding; Complex; Coupled; Crystallography; DNA; DNA Binding; DNA Binding Domain; Funding; Genetic Transcription; Grant; L-Selenomethionine; Light; National Center for Research Resources; Nucleosome Core Particle; Nucleosomes; Phase; Principal Investigator; Relative (related person); Research; Research Infrastructure; Resolution; Resources; Slide; Source; Structure; Synchrotrons; United States National Institutes of Health; Yeasts; chromatin remodeling; cost

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Chd1 is a chromatin remodeler that participates in gene transcription by manipulating nucleosome structure. By sliding nucleosomes along DNA, Chd1 is known to generate evenly-spaced nucleosomal arrays, and we have found that the Chd1 DNA-binding domain is essential for sensing the relative distances between nucleosomes. The Chd1 DNA-binding domain binds DNA in a sequence-nonspecific fashion, and current questions include (1) how the DNA-binding domain interacts with DNA just outside the nucleosome core, (2) whether binding is coupled to conformational changes in the DNA duplex, and (3) whether DNA binding by Chd1 would be expected to be compatible with DNA associating with the nucleosome (i.e. promote release of the DNA-binding domain). We currently have crystals of the yeast Chd1 DNA-binding domain in complex with a 12mer DNA duplex that diffract to better than 2.3 angstrom resolution. We have grown small SeMet crystals and hope to obtain phases and solve the structure.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 CHD1是一种染色质重塑，通过操纵核小体结构来参与基因转录。通过沿着DNA的滑动核小体，CHD1已知会产生均匀间隔的核小体阵列，我们发现CHD1 DNA结合域对于感知核小体之间的相对距离至关重要。 CHD1 DNA结合结构域以序列非特异性的方式结合DNA，当前问题包括（1）DNA结合域如何与核小体核心外DNA相互作用，（2）结合是否与DNA的构象变化偶联双链体，（3）CHD1结合的DNA是否与与核小体相关的DNA兼容（即促进DNA结合结构域的释放）。目前，我们在复合物中具有酵母CHD1 DNA结合结构域的晶体，具有12mer DNA双链体，衍射率高于2.3 Angstrom分辨率。我们已经种植了小的Semet晶体，并希望获得相位并解决结构。