Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- antigeny nádorové chemie genetika metabolismus MeSH
- apoptóza * MeSH
- buněčné jádro enzymologie patologie MeSH
- časové faktory MeSH
- DNA vazebné proteiny chemie genetika metabolismus MeSH
- DNA-topoisomerasy typu II chemie genetika metabolismus MeSH
- endodeoxyribonukleasy chemie genetika metabolismus MeSH
- HeLa buňky MeSH
- histony chemie genetika metabolismus MeSH
- interakční proteinové domény a motivy MeSH
- konfokální mikroskopie MeSH
- konformace proteinů MeSH
- lidé MeSH
- mapování interakce mezi proteiny MeSH
- molekulární modely MeSH
- rekombinantní fúzní proteiny metabolismus MeSH
- restrukturace chromatinu * MeSH
- rezonanční přenos fluorescenční energie MeSH
- transfekce MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- antigeny nádorové MeSH
- DNA vazebné proteiny MeSH
- DNA-topoisomerasy typu II MeSH
- endodeoxyribonukleasy MeSH
- endonuclease G MeSH Prohlížeč
- histony MeSH
- rekombinantní fúzní proteiny MeSH
Apoptosis is a natural form of cell death involved in many physiological changes in the cell. Defects in the process of apoptosis can lead to serious diseases. During some apoptotic pathways, proteins apoptosis-inducing factor (AIF) and endonuclease G (EndoG) are released from the mitochondria and they translocate into the cell nuclei, where they probably participate in chromatin degradation together with other nuclear proteins. Exact mechanism of EndoG activity in cell nucleus is still unknown. Some interacting partners like flap endonuclease 1, DNase I, and exonuclease III were already suggested, but also other interacting partners were proposed. We conducted a living-cell confocal fluorescence microscopy followed by an image analysis of fluorescence resonance energy transfer to analyze the possibility of protein interactions of EndoG with histone H2B and human DNA topoisomerase II alpha (TOPO2a). Our results show that EndoG interacts with both these proteins during apoptotic cell death. Therefore, we can conclude that EndoG and TOPO2a may actively participate in apoptotic chromatin degradation. The possible existence of a degradation complex consisting of EndoG and TOPO2a and possibly other proteins like AIF and cyclophilin A have yet to be investigated.
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