<br/>Prostate apoptosis response-4 (Par-4) is a pro-apoptotic tumor suppressor protein. This 38 kDa full-length, predominantly intrinsically disordered protein, is cleaved intracellularly by caspase-3 at Asp-131 to generate the 24 kDa functionally active cleaved Par-4 (cl-Par-4) protein. cl-Par-4 inhibits nuclear factor NF-κB-mediated cell survival pathways and causes selective apoptosis in tumor cells. The balance between signals involved in cell survival pathways and tumor suppression pathways are crucial in tumor initiation, progression, and metastasis. Conformational flexibility in intrinsically disordered proteins (IDPs) as well as intrinsically disordered region (IDRs) of proteins provide greater opportunities to these proteins in binding with their targets which can be modulated by acquiring various ensembles under different ionic and other environmental conditions in the cellular milieu.<br/>Using biophysical techniques such as circular dichroism (CD), spectroscopy, dynamic light scattering (DLS), size exclusion chromatography with multi-angle light scattering (SEC-MALS), and intrinsic tyrosine fluorescence, we have demonstrated that the presence of divalent cation (MgCl<sub>2</sub>) increases percent helical content in the structure of cl-Par-4 protein thereby increasing the defined structure in the intrinsically disordered region of this protein. Additional results revealing the effect of other divalent cations on the conformational change in cl-Par-4 will be presented. The acquisition of structure by this IDP under varying ionic conditions is being investigated as a potentially crucial additional level of post-translational control.

Role of cations in the conformational change of caspase-cleaved Par-4 (cl-Par-4) tumor suppressor protein

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.