SOLUTION STRUCTURE DYNAMICS ON DUTPASE

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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.