Přehled o publikaci

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 and then they translocate into the cell nuclei, where they participate in chromatin degradation in a caspase-independent way. The C. elegans homolog of AIF was shown to induce apoptosis and to interact with a homolog of EndoG and together they mediated chromatin DNA degradation. 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. These results offer an important insight into the mechanism of apoptotic cell death, which plays a major role in development and progression of degenerative diseases, cancer, and inflammation.