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https://doi.org/10.1371/journal.pgen.1003830
Title: | Binding of NF-κB to Nucleosomes: Effect of Translational Positioning, Nucleosome Remodeling and Linker Histone H1 | Authors: | Lone I.N. Shukla M.S. Charles Richard J.L. Peshev Z.Y. Dimitrov S. Angelov D. |
Keywords: | cell DNA histone H1 histone H2A histone H2B homodimer immunoglobulin enhancer binding protein nucleosomal DNA RNA unclassified drug animal cell article binding site cell interaction chicken chromatin structure controlled study erythrocyte gel mobility shift assay gene gene sequence nonhuman nucleosome nucleosome remodeling position effect protein binding protein footprinting protein localization RNA translation sequence analysis transcription regulation translational positioning ultraviolet radiation Animals Binding Sites Chromatin Dimerization DNA-Binding Proteins Histones Mi-2 Nucleosome Remodeling and Deacetylase Complex NF-kappa B Nucleosomes Protein Binding Protein Biosynthesis Ultraviolet Rays Xenopus |
Issue Date: | 2013 | Publisher: | Public Library of Science | Citation: | Lone I.N., Shukla M.S., Charles Richard J.L., Peshev Z.Y., Dimitrov S., Angelov D. (2013). Binding of NF-κB to Nucleosomes: Effect of Translational Positioning, Nucleosome Remodeling and Linker Histone H1. PLoS Genetics 9 (9) : e1003830. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pgen.1003830 | Abstract: | NF-κB is a key transcription factor regulating the expression of inflammatory responsive genes. How NF-κB binds to naked DNA templates is well documented, but how it interacts with chromatin is far from being clear. Here we used a combination of UV laser footprinting, hydroxyl footprinting and electrophoretic mobility shift assay to investigate the binding of NF-κB to nucleosomal templates. We show that NF-κB p50 homodimer is able to bind to its recognition sequence, when it is localized at the edge of the core particle, but not when the recognition sequence is at the interior of the nucleosome. Remodeling of the nucleosome by the chromatin remodeling machine RSC was not sufficient to allow binding of NF-κB to its recognition sequence located in the vicinity of the nucleosome dyad, but RSC-induced histone octamer sliding allowed clearly detectable binding of NF-κB with the slid particle. Importantly, nucleosome dilution-driven removal of H2A-H2B dimer led to complete accessibility of the site located close to the dyad to NF-κB. Finally, we found that NF-κB was able to displace histone H1 and prevent its binding to nucleosome. These data provide important insight on the role of chromatin structure in the regulation of transcription of NF-κB dependent genes. © 2013 Lone et al. | Source Title: | PLoS Genetics | URI: | https://scholarbank.nus.edu.sg/handle/10635/165402 | ISSN: | 15537390 | DOI: | 10.1371/journal.pgen.1003830 |
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