McDaniel D, Caplan A J, Lee M S, Adams C C, Fishel B R, Gross D S, Garrard W T
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
Mol Cell Biol. 1989 Nov;9(11):4789-98. doi: 10.1128/mcb.9.11.4789-4798.1989.
Previous studies have shown that heat shock factor is constitutively bound to heat shock elements in Saccharomyces cerevisiae. We demonstrate that mutation of the heat shock element closest to the TATA box of the yeast HSP82 promoter abolishes basal-level transcription without markedly affecting inducibility. The mutated heat shock element no longer bound putative heat shock factor, either in vitro or in vivo, but still resided within a nuclease-hypersensitive site in the chromatin. Thus, constitutive binding of heat shock factor to heat shock elements in S. cerevisiae appears to functionally direct basal-level transcription.
先前的研究表明,热休克因子在酿酒酵母中与热休克元件组成性结合。我们证明,酵母HSP82启动子中最靠近TATA盒的热休克元件发生突变会消除基础水平的转录,而不会显著影响诱导性。无论是在体外还是体内,突变的热休克元件都不再与假定的热休克因子结合,但仍位于染色质中的核酸酶超敏位点内。因此,热休克因子与酿酒酵母中热休克元件的组成性结合似乎在功能上指导基础水平的转录。