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The Hsp90 molecular chaperone system

Hsp90分子伴侣系统

基本信息

批准号：
9256500
负责人：
Brian C Freeman
金额：
$ 35.17万
依托单位：
UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN
依托单位国家：
美国
项目类别：
财政年份：
2011
资助国家：
美国
起止时间：
2011-07-12 至 2020-04-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/9256500
关键词：
Address Area Behavior Binding Biochemical Biological Assay Biological Preservation Biology Cell Nucleus Cells Characteristics Chromatin Chromatin Structure Chromosomes Client Complex DNA DNA Structure Data Defect Disease Elements Environment Event Gene Expression Regulation Genetic Genetic study Genome Goals Health Homeostasis Human In Vitro Individual Joints Life Cycle Stages Link Maintenance Mediating Molecular Molecular Chaperones Molecular Models Monitor Nuclear Nucleosomes Outcome Physiological Pliability Process Protein Complex Subunit Protein Subunits Proteins Recruitment Activity Regulation Research Research Proposals Role Structure System Testing Work chromatin remodeling combinatorial in vivo inhibitor/antagonist molecular modeling novel protein complex protein structure public health relevance transcription factor yeast genome

项目摘要

DESCRIPTION (provided by applicant): Our long-term objectives are to understand the Hsp90 molecular chaperone system from physiological relevance to mechanistic action. Molecular chaperones are typically identified with the beginning (folding) and ending (degradation) of the protein life cycle. Yet, chaperones in the Hsp90 system are often associated with native proteins including assembled structures. The significance of chaperone interactions with seemingly native proteins is poorly understood. We will exploit our discoveries connecting the Hsp90 system to chromatin modifiers to determine why certain chaperones interact with select native proteins. Our current plans will resolve how molecular chaperones cooperatively modulate multi-subunit protein complexes. To achieve our goal we are exploiting chromatin remodelers as molecular models. In brief, we are investigating the individual and joint regulatory effects of Hsp90 and p23 on nucleosome remodeling process. Our plans will define how Hsp90 controls select chromatin remodelers, will identify the joint impact of Hsp90 and p23 on remodelers, will determine the impact of Hsp90 on the chromatin landscape, and will show how the control of chromatin remodelers by Hsp90 and p23 supports homeostasis.

描述（由申请人提供）：我们的长期目标是了解Hsp90分子伴侣系统从生理相关性到机械作用。分子伴侣通常与蛋白质生命周期的开始（折叠）和结束（降解）有关。然而，Hsp90系统中的分子伴侣通常与天然蛋白质（包括组装结构）相关。分子伴侣与看似天然的蛋白质相互作用的重要性知之甚少。我们将利用我们的发现连接热休克蛋白90系统染色质修饰剂，以确定为什么某些分子伴侣与选择天然蛋白质相互作用。我们目前的计划将解决分子伴侣如何协同调节多亚基蛋白质复合物。为了实现我们的目标，我们正在利用染色质重塑分子模型。总之，我们正在研究Hsp90和p23对核小体重塑过程的单独和联合调节作用。我们的计划将定义Hsp90如何控制选择染色质重塑，将确定Hsp90和p23对重塑的联合影响，将确定Hsp90对染色质景观的影响，并将显示Hsp90和p23如何控制染色质重塑支持稳态。