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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F12%3A00059138" target="_blank" >RIV/00216224:14330/12:00059138 - isvavai.cz</a>

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs11010-011-1182-x" target="_blank" >http://link.springer.com/article/10.1007%2Fs11010-011-1182-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11010-011-1182-x" target="_blank" >10.1007/s11010-011-1182-x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 othernuclear proteins. Exact mechanism of EndoG activity in cell nucleus is still unknown. We conducted a living-cell confocal fluorescence microscopy followed by an image analysis of fluorescence resonance energy transfer (FRET) 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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 othernuclear proteins. Exact mechanism of EndoG activity in cell nucleus is still unknown. We conducted a living-cell confocal fluorescence microscopy followed by an image analysis of fluorescence resonance energy transfer (FRET) 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Mol Cell Biochem

ISSN

0300-8177

e-ISSN

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Svazek periodika

363

Číslo periodika v rámci svazku

1-2

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

7

Strana od-do

301-307

Kód UT WoS článku

000300888900030

EID výsledku v databázi Scopus

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