Interaction of endonuclease G with histone H2B, AIF, and DNA topoisomerase II alpha during apoptosis as revealed by FRET imaging of living cells
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| Year of publication | 2011 |
| Type | Conference abstract |
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| Description | Apoptosis is a natural form of cell death involved in many physiological changes in the cell. During some forms of cell death, proteins endonuclease G (EndoG) and apoptosis-inducing factor (AIF) are released from mitochondria, then they translocate into the cell nuclei, where they participate in chromatin degradation in a caspase-independent way. We have conducted living-cell confocal fluorescence microscopy followed by analysis of fluorescence resonance energy transfer (FRET) to observe the protein interaction of EndoG with AIF and their interactions with other proteins in human cell nuclei after induction of apoptosis. Our results show that EndoG interacts with histone H2B, AIF, and DNA topoisomerase II alpha (TOPO2a). Also AIF was found to interact with TOPO2a. Therefore we can conclude that EndoG, AIF, and TOPO2a may form a protein complex allowing chromatin degradation in apoptotic nucleus. |
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