Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a

Specific combinations of post-translational modifications of histones alter chromatin structure, facilitating gene transcription or silencing. Here we have investigated the 'histone code' associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification...

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Detalles Bibliográficos
Autores principales: Robin, Philippe, Fritsch, Lauriane, Philipot, Ophélie, Svinarchuk, Fedor, Ait-Si-Ali, Slimane
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Method
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246272/
https://www.ncbi.nlm.nih.gov/pubmed/18096052
http://dx.doi.org/10.1186/gb-2007-8-12-r270
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author Robin, Philippe
Fritsch, Lauriane
Philipot, Ophélie
Svinarchuk, Fedor
Ait-Si-Ali, Slimane
author_facet Robin, Philippe
Fritsch, Lauriane
Philipot, Ophélie
Svinarchuk, Fedor
Ait-Si-Ali, Slimane
author_sort Robin, Philippe
collection PubMed
description Specific combinations of post-translational modifications of histones alter chromatin structure, facilitating gene transcription or silencing. Here we have investigated the 'histone code' associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification and mass spectrometry. Our results confirm the previously reported histone modifications associated with Suv39h1 and G9a. Moreover, this method allowed us to demonstrate for the first time an association of acetylated histones with the repressor proteins Suv39h1 and G9a.
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spelling pubmed-22462722008-02-20 Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a Robin, Philippe Fritsch, Lauriane Philipot, Ophélie Svinarchuk, Fedor Ait-Si-Ali, Slimane Genome Biol Method Specific combinations of post-translational modifications of histones alter chromatin structure, facilitating gene transcription or silencing. Here we have investigated the 'histone code' associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification and mass spectrometry. Our results confirm the previously reported histone modifications associated with Suv39h1 and G9a. Moreover, this method allowed us to demonstrate for the first time an association of acetylated histones with the repressor proteins Suv39h1 and G9a. BioMed Central 2007 2007-12-20 /pmc/articles/PMC2246272/ /pubmed/18096052 http://dx.doi.org/10.1186/gb-2007-8-12-r270 Text en Copyright © 2008 Robin et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Method
Robin, Philippe
Fritsch, Lauriane
Philipot, Ophélie
Svinarchuk, Fedor
Ait-Si-Ali, Slimane
Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title_full Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title_fullStr Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title_full_unstemmed Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title_short Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a
title_sort post-translational modifications of histones h3 and h4 associated with the histone methyltransferases suv39h1 and g9a
topic Method
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246272/
https://www.ncbi.nlm.nih.gov/pubmed/18096052
http://dx.doi.org/10.1186/gb-2007-8-12-r270
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