Analysis of the mechanism of eukaryotic transcription initiation and its regulation based on the TATA box-binding factor TFIID

点击翻译按钮获取中文摘要

TATA box-binding factor TFIID plays a crucial role in machanisms of transcription activation. We elucidated the significance of function and structure of TFIID in eukaryotic transcription initiation and its regulation by several methods.1. Mechanism of the transcriptional activation through the competitive binding of Drosophila TAF_<II>230 and the transcriptional activator VP162. Functional analysis of specific interactions of human TAF_<II>100, one of the TFIID subunit3. Analysis of the involvement of the histone fold motifs in the mutual interaction between human TAF_<II>80 and TAF_<II>224. Analysis of restricted expression of a member of the transcription elongation factor S-II family in testicular germ cells during and after meiosis5. Molecular genetic elucidation of the tripartite structure of the Schizosaccharomyces pombe 72 kDa TFIID subunit which contains a WD40 structural motif6. Elucidation of novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip607. Elucidation of defect in cytokinesis of fission yeast induced by mutation in the WD40 repeat motif of a TFIID subunit8. Hypothesis of mechanism of how histone acetyltransferases select lysine residues in core histones9. Isolation and initial characterization of GBF ; a novel DNA-binding zinc finger protein that binds to the GC-rich binding sites of the HIV-1 promoter10. Analysis of acetylation of six lysines of a specific class by Tip 60 in core histones in vitro11. Analysis of TFIIH subunit, through isolation of the gene from Schizosaccharomyces pombe corresponding to that of Saccharomyces cerevisiae SSL1, reveals the presence of conserved structural motifs