Nucleic Acids Research Advance Access originally published online on December 19, 2006
Nucleic Acids Research 2007 35(3):705-715; doi:10.1093/nar/gkl1077
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Nucleic Acids Research, 2007, Vol. 35, No. 3 705-715
© 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.
Molecular Biology |
Histone acetylation-independent transcription stimulation by a histone chaperone
Department of Infection Biology, Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba 1-1-1 Tennodai, Tsukuba 305-8575, Japan
*To whom correspondence should be addressed. Tel: +81 29 853 3233; Fax: +81 29 853 3233; Email: knagata{at}md.tsukuba.ac.jp
Received August 21, 2006. Revised October 31, 2006. Accepted November 21, 2006.
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.
Present address: Mary Miyaji-Yamaguchi, Department of Neuroanatomy and Neurobiology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, 2-5-1 Shikata-cho, Okayama 700-8558, Japan
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