In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP

Nucleolin is a major nucleolar protein involved in various aspects of ribosome biogenesis such as regulation of polymerase I transcription, pre-RNA maturation, and ribosome assembly. Nucleolin is also present in the nucleoplasm suggesting that its functions are not restricted to nucleoli. Nucleolin...

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Main Authors: Xavier Gaume, Karine Monier, Françoise Argoul, Fabien Mongelard, Philippe Bouvet
Format: Article
Language:English
Published: Wiley 2011-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2011/187624
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author Xavier Gaume
Karine Monier
Françoise Argoul
Fabien Mongelard
Philippe Bouvet
author_facet Xavier Gaume
Karine Monier
Françoise Argoul
Fabien Mongelard
Philippe Bouvet
author_sort Xavier Gaume
collection DOAJ
description Nucleolin is a major nucleolar protein involved in various aspects of ribosome biogenesis such as regulation of polymerase I transcription, pre-RNA maturation, and ribosome assembly. Nucleolin is also present in the nucleoplasm suggesting that its functions are not restricted to nucleoli. Nucleolin possesses, in vitro, chromatin co-remodeler and histone chaperone activities which could explain numerous functions of nucleolin related to the regulation of gene expression. The goal of this report was to investigate the consequences of nucleolin depletion on the dynamics of histones in live cells. Changes in histone dynamics occurring in nucleolin silenced cells were measured by FRAP experiments on eGFP-tagged histones (H2B, H4, and macroH2A). We found that nuclear histone dynamics was impacted 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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spelling doaj-art-f5df499b39fb4cbfaa158c98cf9169c22025-02-03T01:11:17ZengWileyBiochemistry Research International2090-22472090-22552011-01-01201110.1155/2011/187624187624In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAPXavier Gaume0Karine Monier1Françoise Argoul2Fabien Mongelard3Philippe Bouvet4Université de Lyon, Laboratoire Joliot-Curie, Centre National de la Recherche Scientifique (CNRS)/Ecole Normale Supérieure de Lyon, 69007 Lyon, FranceUniversité de Lyon, Laboratoire Joliot-Curie, Centre National de la Recherche Scientifique (CNRS)/Ecole Normale Supérieure de Lyon, 69007 Lyon, FranceUniversité de Lyon, Laboratoire Joliot-Curie, Centre National de la Recherche Scientifique (CNRS)/Ecole Normale Supérieure de Lyon, 69007 Lyon, FranceUniversité de Lyon, Laboratoire Joliot-Curie, Centre National de la Recherche Scientifique (CNRS)/Ecole Normale Supérieure de Lyon, 69007 Lyon, FranceUniversité de Lyon, Laboratoire Joliot-Curie, Centre National de la Recherche Scientifique (CNRS)/Ecole Normale Supérieure de Lyon, 69007 Lyon, FranceNucleolin is a major nucleolar protein involved in various aspects of ribosome biogenesis such as regulation of polymerase I transcription, pre-RNA maturation, and ribosome assembly. Nucleolin is also present in the nucleoplasm suggesting that its functions are not restricted to nucleoli. Nucleolin possesses, in vitro, chromatin co-remodeler and histone chaperone activities which could explain numerous functions of nucleolin related to the regulation of gene expression. The goal of this report was to investigate the consequences of nucleolin depletion on the dynamics of histones in live cells. Changes in histone dynamics occurring in nucleolin silenced cells were measured by FRAP experiments on eGFP-tagged histones (H2B, H4, and macroH2A). We found that nuclear histone dynamics was impacted 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.http://dx.doi.org/10.1155/2011/187624
spellingShingle Xavier Gaume
Karine Monier
Françoise Argoul
Fabien Mongelard
Philippe Bouvet
In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
Biochemistry Research International
title In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
title_full In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
title_fullStr In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
title_full_unstemmed In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
title_short In vivo Study of the Histone Chaperone Activity of Nucleolin by FRAP
title_sort in vivo study of the histone chaperone activity of nucleolin by frap
url http://dx.doi.org/10.1155/2011/187624
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