S CEREVISIAE GENERAL TRANSCRIPTION FACTOR TFIID

酿酒酵母通用转录因子TFIID

• 批准号: 7953770
• 负责人: RAYMOND H JACOBSON
• 金额: $ 2.61万
• 依托单位: BAYLOR COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-12-01 至 2009-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7953770
• 关键词: Affinity Chromatography; Complex; Computer Retrieval of Information on Scientific Projects Database; Data; Defect; Development; Electron Microscopy; Funding; Gene Expression Regulation; General Transcription Factors; Genetic Transcription; Goals; Grant; Individual; Institution; Malignant Neoplasms; Metabolic Diseases; Negative Staining; Organism; Proteins; RNA Polymerase II; Research; Research Personnel; Resolution; Resources; Roentgen Rays; Site; Solubility; Source; Structure; System; Transcription Factor TFIID; United States National Institutes of Health; Yeasts; interest; macromolecule; promoter; reconstruction; spatial relationship

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. Transcription factor TFIID is a multi-subunit complex responsible for targeting and nucleating the assembly of RNA polymerase II and other associated factors to promoter start sites in eukaryotic organisms. It is important for the regulation of gene expression. Mis-regulation of gene expression can cause developmental defects, metabolic disorders, and cancer. Understanding the mechanism of transcriptional initiation is an important goal, and structural information about TFIID would contribute towards this end. The TFIID complex is estimated to contain 1.1-1.2 MDa of protein contributed from 15 individual subunits. Structural information for this large complex has been difficult to obtain due to expression and solubility problems for the isolated subunits and difficulty in obtaining sufficient material. Our goal has been to extend on negative stain electron microscopy studies of the yeast TFIID complex carried out by the group of P. Schultz using Tandem Affinity Purification (TAP-tag) isolated material. We will obtain cryo-EM reconstructions of the TFIID complex. This data will be used in our efforts to obtaining a high-resolution X-ray crystal structure. It would be of particular interest to further characterize the interactions of TFIID with other known basal factors using cryo-EM to further reveal the spatial relationships between the various components of the RNA Polymerase II transcription system at promoters.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此，可以在其他清晰的条目中表示。列出的机构是 对于中心，这不一定是调查员的机构。 转录因子TFIID是一种多生子络合物，负责靶向和成核RNA聚合酶II和其他相关因素和其他相关因素，以促进真核生物中的启动子起始位点。这对于调节基因表达很重要。基因表达的错误调节会导致发育缺陷，代谢性疾病和癌症。了解转录启动的机制是一个重要的目标，有关TFIID的结构信息将有助于这一目标。据估计，TFIID复合物含有1.1-1.2 MDA的蛋白质，源自15个单个亚基。由于孤立亚基的表达和溶解度问题以及获得足够的材料的困难，因此很难获得该大型复合物的结构信息。我们的目标是使用P. Schultz组进行的酵母TFIID复合物进行负染色电子显微镜研究，并使用串联亲和力纯化（TAP-TAG）隔离材料进行。我们将获得TFIID复合物的冷冻EM重建。这些数据将用于我们获得高分辨率X射线晶体结构的努力。进一步表征TFIID与其他已知基础因素的相互作用使用Cryo-EM的相互作用，以进一步揭示启动子RNA聚合酶II转录系统的各种成分之间的空间关系。