SOLUTION STRUCTURE DYNAMICS ON DUTPASE

DUTPASE 的解决方案结构动力学

• 批准号: 7370663
• 负责人: HIDEAKI MORIYAMA
• 金额: $ 0.13万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370663
• 关键词: SOLUTION; STRUCTURE; DYNAMICS; DUTPASE

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. Elucidate the molecular mechanisms of the temperature optima shift. Two deoxyuridine triphosphate nucleotidohydrolase (dUTPases) of the chlorella virus, with low and high temperature optima, respectively, will be compared in terms of solution structure, structural kinetics, and enzymatic activity. This enzyme involves in a typical example of horizontal transfer of the gene, which mimics development of cancers. Lack of dUTPase activity initiates thymine-less cell death. A detailed understanding of the mechanism and cellular role of the enzyme will offer novel means to modulate thymine-less apoptosis. Once it is known how temperature influences adaptation of dUPTase and its role in regulating development of cancer cells, the door may open to new and innovative approaches to preventing and treating cancers.

该子项目是利用 NIH/NCRR 资助的中心拨款提供的资源的众多研究子项目之一。子项目和研究者 (PI) 可能已从另一个 NIH 来源获得主要资金，因此可以在其他 CRISP 条目中得到体现。列出的机构是中心的机构，不一定是研究者的机构。阐明最佳温度变化的分子机制。小球藻病毒的两种脱氧尿苷三磷酸核苷酸水解酶（dUTPases）分别具有低温和高温最佳温度，将在溶液结构、结构动力学和酶活性方面进行比较。这种酶涉及基因水平转移的典型例子，模拟癌症的发展。缺乏 dUTPase 活性会引发无胸腺嘧啶的细胞死亡。详细了解该酶的机制和细胞作用将为调节无胸腺嘧啶凋亡提供新方法。一旦了解温度如何影响 dUPTase 的适应及其在调节癌细胞发育中的作用，就有可能为预防和治疗癌症的创新方法打开大门。