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Effect of FRAP on histone chaperone activity of nucleolar protein in vivo

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Document pages: 15 pages

Abstract: Nucleolar protein is a major nucleolar protein, which is involved in all aspects of ribosome biogenesis, such as the regulation of polymerase I transcription, RNA precursor maturation and ribosome assembly. Nucleolar protein also exists in nucleoplasm, indicating that its function is not limited to nucleolus. Nucleolar proteins have chromatin co remodeling and histone chaperone activity in vitro, which can explain many functions of nucleolar proteins related to gene expression regulation. The purpose of this report is to study the effect of nucleolar protein deletion on histone dynamics in living cells. The histone dynamics changes in nucleolar protein silenced cells were measured by FRAP experiment on EGFP labeled histones (H2B, H4 and macroH2A). We found that nuclear histone dynamics was affectedd in nucleolin silenced cells; in particular we measured higher fluorescence recovery kinetics for macroH2A and H2B but not for H4. Interestingly, we showed that nucleolin depletion also impacted the dissociation constant rate of H2B and H4. Thus, in live cells, nucleolin could play a role in chromatin accessibility by its histone chaperone and co-remodeling activities.

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