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Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis

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Abstract

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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Acknowledgment

This work was supported by The Ministry of Education, Youth and Sports of the Czech Republic (project numbers: 2B06052, LC535, and MSM0021622419).

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Authors and Affiliations

  1. Centre for Biomedical Image Analysis, Faculty of Informatics, Masaryk University, Botanická 68a, 602 00, Brno, Czech Republic

    Miroslav Vařecha, Michaela Potěšilová, Pavel Matula & Michal Kozubek

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  1. Miroslav Vařecha
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  2. Michaela Potěšilová
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  3. Pavel Matula
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  4. Michal Kozubek
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Correspondence to Miroslav Vařecha.

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Vařecha, M., Potěšilová, M., Matula, P. et al. Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis. Mol Cell Biochem 363, 301–307 (2012). https://doi.org/10.1007/s11010-011-1182-x

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  • DOI: https://doi.org/10.1007/s11010-011-1182-x

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