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Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin
G. Sustáčková, S. Kozubek, L. Stixová, S. Legartová, P. Matula, D. Orlova, E. Bártová,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Medline Complete (EBSCOhost)
od 2005-06-01 do Před 1 rokem
Wiley Online Library (archiv)
od 1996-01-01 do 2012-12-31
PubMed
21732356
DOI
10.1002/jcp.22912
Knihovny.cz E-zdroje
- MeSH
- acetylace MeSH
- buněčné linie MeSH
- buňky 3T3 MeSH
- časosběrné zobrazování MeSH
- chromatin metabolismus účinky záření MeSH
- chromozomální proteiny, nehistonové genetika metabolismus MeSH
- FRAP MeSH
- histony metabolismus MeSH
- inhibitory histondeacetylas metabolismus MeSH
- jaderné proteiny genetika metabolismus MeSH
- konfokální mikroskopie metody MeSH
- kyseliny hydroxamové metabolismus MeSH
- lidé MeSH
- myši MeSH
- poškození DNA MeSH
- protoonkogenní proteiny genetika metabolismus MeSH
- rekombinantní fúzní proteiny genetika metabolismus MeSH
- represorové proteiny genetika metabolismus MeSH
- ultrafialové záření MeSH
- zelené fluorescenční proteiny genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Polycomb group (PcG) proteins, organized into Polycomb bodies, are important regulatory components of epigenetic processes involved in the heritable transcriptional repression of target genes. Here, we asked whether acetylation can influence the nuclear arrangement and function of the BMI1 protein, a core component of the Polycomb group complex, PRC1. We used time-lapse confocal microscopy, micro-irradiation by UV laser (355 nm) and GFP technology to study the dynamics and function of the BMI1 protein. We observed that BMI1 was recruited to UV-damaged chromatin simultaneously with decreased lysine acetylation, followed by the recruitment of heterochromatin protein HP1β to micro-irradiated regions. Pronounced recruitment of BMI1 was rapid, with half-time τ = 15 sec; thus, BMI1 is likely involved in the initiation step leading to the recognition of UV-damaged sites. Histone hyperacetylation, stimulated by HDAC inhibitor TSA, suppression of transcription by actinomycin D, and ATP-depletion prevented increased accumulation of BMI1 to γH2AX-positive irradiated chromatin. Moreover, BMI1 had slight ability to recognize spontaneously occurring DNA breaks caused by other pathophysiological processes. Taken together, our data indicate that the dynamics of recognition of UV-damaged chromatin, and the nuclear arrangement of BMI1 protein can be influenced by acetylation and occur as an early event prior to the recruitment of HPβ to UV-irradiated chromatin.
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- $a Polycomb group (PcG) proteins, organized into Polycomb bodies, are important regulatory components of epigenetic processes involved in the heritable transcriptional repression of target genes. Here, we asked whether acetylation can influence the nuclear arrangement and function of the BMI1 protein, a core component of the Polycomb group complex, PRC1. We used time-lapse confocal microscopy, micro-irradiation by UV laser (355 nm) and GFP technology to study the dynamics and function of the BMI1 protein. We observed that BMI1 was recruited to UV-damaged chromatin simultaneously with decreased lysine acetylation, followed by the recruitment of heterochromatin protein HP1β to micro-irradiated regions. Pronounced recruitment of BMI1 was rapid, with half-time τ = 15 sec; thus, BMI1 is likely involved in the initiation step leading to the recognition of UV-damaged sites. Histone hyperacetylation, stimulated by HDAC inhibitor TSA, suppression of transcription by actinomycin D, and ATP-depletion prevented increased accumulation of BMI1 to γH2AX-positive irradiated chromatin. Moreover, BMI1 had slight ability to recognize spontaneously occurring DNA breaks caused by other pathophysiological processes. Taken together, our data indicate that the dynamics of recognition of UV-damaged chromatin, and the nuclear arrangement of BMI1 protein can be influenced by acetylation and occur as an early event prior to the recruitment of HPβ to UV-irradiated chromatin.
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