Prediction of localization and interactions of proteins involved in caspase-independent apoptosis
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| Year of publication | 2009 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein is AIF-homologous mitochondrion-associated inducer of death (AMID). Heat shock protein HSP70-1, cyclophilin A and possibly DNA topoisomerase II alpha are also high candidate proteins that seem to take part at least in some part of caspase-independent apoptosis connected to AIF. We studied the structure, cellular localization, and interactions of these proteins in silico and also in cells using fluorescent microscopy. Bioinformatic predictions were conducted to analyze the interactions of some of the studied proteins with possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions. Our results show data acquired using a combination of modern in silico methods and image analysis to understand the localization, interactions and functions of proteins AMID, AIF, endonuclease G, HSP70-1, DNA topoisomerase II alpha and cyclophilin A in caspase-independent apoptosis. |
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