SOLUTION STRUCTURE DYNAMICS ON DUTPASE

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。阐明温度最优转移的分子机制。将小球藻病毒的两种脱氧尿嘧啶三磷酸核苷酸水解酶（dutpase）分别在低温和高温条件下进行溶液结构、结构动力学和酶活性的比较。这种酶参与了一个典型的基因水平转移的例子，它模仿了癌症的发展。dUTPase活性的缺乏引发胸腺嘧啶缺失的细胞死亡。详细了解该酶的机制和细胞作用将为调节无胸腺嘧啶细胞凋亡提供新的手段。一旦了解温度如何影响dUPTase的适应性及其在调节癌细胞发育中的作用，就可能为预防和治疗癌症的新方法和创新方法打开大门。

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.