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Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin

Basic information
Original title:Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin
Authors:Gabriela Šustáčková, Stanislav Kozubek, Lenka Stixová, Soňa Legartová, Pavel Matula, Darya Yurevna Orlova, Eva Bártová
Further information
Citation:ŠUSTÁČKOVÁ, Gabriela, Stanislav KOZUBEK, Lenka STIXOVÁ, Soňa LEGARTOVÁ, Pavel MATULA, Darya Yurevna ORLOVA and Eva BÁRTOVÁ. Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin (Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin). Journal of cellular physiology, United States: Wiley-Liss, 2012, vol. 227, No 5, p. 1838-1850. ISSN 0021-9541. doi:10.1002/jcp.22912.Export BibTeX
@article{952094,
author = {Šustáčková, Gabriela and Kozubek, Stanislav and Stixová, Lenka and Legartová, Soňa and Matula, Pavel and Orlova, Darya Yurevna and Bártová, Eva},
article_location = {United States},
article_number = {5},
doi = {http://dx.doi.org/10.1002/jcp.22912},
keywords = {Polycomb body BMI1 protein arrangement confocal microscopy},
language = {eng},
issn = {0021-9541},
journal = {Journal of cellular physiology},
title = {Acetylation-dependent nuclear arrangement and recruitment of BMI1 protein to UV-damaged chromatin},
url = {http://onlinelibrary.wiley.com/doi/10.1002/jcp.22912/suppinfo},
volume = {227},
year = {2012}
}
Original language:English
Field:Genetics and molecular biology
WWW:link to a new windowhttp://onlinelibrary.wiley.com/doi/10.1002/jcp.22912/suppinfo
Type:Article in Periodical
Keywords:Polycomb body BMI1 protein arrangement confocal microscopy

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. 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 HPb to UV-irradiated chromatin.

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