Tumor suppressor proteins are responsible for important cellular functions, such as DNA repair and cell apoptosis. Prostate apoptosis response 4 (Par-4) is a 38kDa tumor suppressor protein that has been shown to induce cell apoptosis in response to various stimuli in different cellular systems. However, Par-4 is a largely intrinsically disordered protein under neutral conditions <i>in vitro</i>. Hence, investigating how Par-4 folds under various conditions will increase our understanding of Par-4 structure and how it may be related to function.<br/>Full-length (FL) Par-4 translocates into the nucleus for cell apoptosis induction only after it is cleaved by the caspase-3 at aspartic acid 131. Previous research of the caspase-3 cleaved fragment (cl- Par-4) have shown that ordered protein structure can be induced by either acidic conditions or by a high concentration of monovalent cations. In this study, we are investigating whether similar conditions also induce structure into full-length (FL) Par-4. Determining FL Par-4 structure will enhance our understanding of structural similarities and differences between the FL Par-4 and cl-Par-4 fragment, and help to clarify the role of caspase-induced cleavage of Par-4 in apoptosis. Preliminary circular dichroism (CD) data of FL Par-4 show that both monovalent and divalent cations do affect the degree of structure in FL-Par-4. A full analysis of these effects will be presented. Additional techniques, such as tyrosine fluorescence, size exclusion chromatography with multi angle scattering (SEC-MALS), and dynamic light scattering (DLS) will also be used to characterize FL Par-4 structure under various conditions. These results will increase our understanding of Par-4 structure in relation to the cellular environment and how cleavage alters Par-4 structure, including the ability of Par-4 to be induced to fold via various stimuli.<br/>

Biophysical characterization of the full-length Par-4 tumor suppressor

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.