Structure and temperature adaptation of chaperonin TF55 from Sulfolobus solfataricus

硫磺硫化叶菌伴侣蛋白 TF55 的结构和温度适应性

• 批准号: DP1093649
• 负责人: Dr Daniela Stock
• 金额: $ 22.98万
• 依托单位: The University of New South Wales
• 依托单位国家: 澳大利亚
• 项目类别: Discovery Projects
• 财政年份: 2010
• 资助国家: 澳大利亚
• 起止时间: 2010-01-01 至 2012-12-31
• 项目状态: 已结题
• 来源: https://dataportal.arc.gov.au/RGS/Web/Grants/DP1093649
• 关键词: Structure; temperature; adaptation; chaperonin; TF55

Our work has future potential both for biotechnology and for medical therapies. The cages formed by chaperonin subunits and their ability to bind to specific targets could lead to their application as nano-vesicles, could facilitate expression of eukaryotic proteins in bacteria and could help to prevent or dissolve protein aggregates. With Australia's ageing population, we can expect an increasing prevalence of pathologies such as Alzheimer's and Parkinson's disease and other diseases that arise from protein mis-folding and aggregation, including myopathies and cataracts. A participation of chaperonins has been implicated in these age-related diseases and demands detailed structural and functional investigations.

我们的工作在生物技术和医学治疗方面都具有未来的潜力。伴侣蛋白亚基形成的笼状结构及其与特定靶点结合的能力可能导致其作为纳米囊泡的应用，可以促进真核蛋白在细菌中的表达，并且可以帮助防止或溶解蛋白质聚集体。随着澳大利亚人口的老龄化，我们可以预期阿尔茨海默氏症和帕金森氏症等病理学以及其他由蛋白质错误折叠和聚集引起的疾病（包括肌病和白内障）的患病率将越来越高。伴侣蛋白的参与已被牵连在这些与年龄有关的疾病，需要详细的结构和功能的调查。