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Histone acetylation-independent transcription stimulation by a histone chaperone
Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807960/ https://www.ncbi.nlm.nih.gov/pubmed/17179179 http://dx.doi.org/10.1093/nar/gkl1077 |
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author | Kato, Kohsuke Miyaji-Yamaguchi, Mary Okuwaki, Mitsuru Nagata, Kyosuke |
author_facet | Kato, Kohsuke Miyaji-Yamaguchi, Mary Okuwaki, Mitsuru Nagata, Kyosuke |
author_sort | Kato, Kohsuke |
collection | PubMed |
description | Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical properties have been well studied. By performing microarray analyses, we found that TAF-I stimulates the transcription of a sub-set of genes. The transcription of endogenous genes that was up-regulated by TAF-I was found to be additively stimulated by histone acetylation. On performing an experiment with a cell line containing a model gene integrated into the chromosome, TAF-I was found to stimulate the model gene transcription in a histone chaperone activity-dependent manner additively with histone acetylation. TAF-I bound to the core histones and remodeled the chromatin structure independent of the N-terminal histone tail and its acetylation level in vitro. These results suggest that TAF-I remodel the chromatin structure through its interaction with the core domain of the histones, including the histone fold, and this mechanism is independent of the histone acetylation status. |
format | Text |
id | pubmed-1807960 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-18079602007-03-02 Histone acetylation-independent transcription stimulation by a histone chaperone Kato, Kohsuke Miyaji-Yamaguchi, Mary Okuwaki, Mitsuru Nagata, Kyosuke Nucleic Acids Res Molecular Biology Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical properties have been well studied. By performing microarray analyses, we found that TAF-I stimulates the transcription of a sub-set of genes. The transcription of endogenous genes that was up-regulated by TAF-I was found to be additively stimulated by histone acetylation. On performing an experiment with a cell line containing a model gene integrated into the chromosome, TAF-I was found to stimulate the model gene transcription in a histone chaperone activity-dependent manner additively with histone acetylation. TAF-I bound to the core histones and remodeled the chromatin structure independent of the N-terminal histone tail and its acetylation level in vitro. These results suggest that TAF-I remodel the chromatin structure through its interaction with the core domain of the histones, including the histone fold, and this mechanism is independent of the histone acetylation status. Oxford University Press 2007-02 2006-12-19 /pmc/articles/PMC1807960/ /pubmed/17179179 http://dx.doi.org/10.1093/nar/gkl1077 Text en © 2006 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Molecular Biology Kato, Kohsuke Miyaji-Yamaguchi, Mary Okuwaki, Mitsuru Nagata, Kyosuke Histone acetylation-independent transcription stimulation by a histone chaperone |
title | Histone acetylation-independent transcription stimulation by a histone chaperone |
title_full | Histone acetylation-independent transcription stimulation by a histone chaperone |
title_fullStr | Histone acetylation-independent transcription stimulation by a histone chaperone |
title_full_unstemmed | Histone acetylation-independent transcription stimulation by a histone chaperone |
title_short | Histone acetylation-independent transcription stimulation by a histone chaperone |
title_sort | histone acetylation-independent transcription stimulation by a histone chaperone |
topic | Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807960/ https://www.ncbi.nlm.nih.gov/pubmed/17179179 http://dx.doi.org/10.1093/nar/gkl1077 |
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