title: Histone acetylation-independent transcription stimulation by a histone chaperone.
abstract: 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.
authors.affiliation: 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.
authors.forename: Kohsuke
authors.initials: K
authors.lastname: Kato
authors.forename: Mary
authors.initials: M
authors.lastname: Miyaji-Yamaguchi
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Okuwaki
authors.forename: Kyosuke
authors.initials: K
authors.lastname: Nagata
mesh_terms: D000107:Acetylation; D000818:Animals; D016466:CHO Cells; D002843:Chromatin / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism* / Q000502:physiology; D006224:Cricetinae; D003412:Cricetulus; D004268:DNA-Binding Proteins; D006367:HeLa Cells; D056488:Histone Chaperones; D006657:Histones / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism* / Q000502:physiology; D014157:Transcription Factors / Q000378:metabolism* / Q000502:physiology; D015533:Transcriptional Activation
chemical_list: D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D056488:Histone Chaperones; D006657:Histones; D018832:Molecular Chaperones; C513473:SET protein, human; D014157:Transcription Factors