Nowak S J, Corces V G
Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
Genes Dev. 2000 Dec 1;14(23):3003-13. doi: 10.1101/gad.848800.
Posttranslational modifications of the N-terminal tails of the core histones within the nucleosome particle are thought to act as signals from the chromatin to the cell for various processes. The experiments presented here show that the acetylation of histones H3 and H4 in polytene chromosomes does not change during heat shock. In contrast, the global level of phosphorylated H3 decreased dramatically during a heat shock, with an observed increase in H3 phosphorylation at the heat shock loci. Additional experiments confirm that this change in phosphorylated H3 distribution is dependent on functional heat shock transcription factor activity. These experiments suggest that H3 phosphorylation has an important role in the induction of transcription during the heat shock response.
核小体颗粒内核心组蛋白N端尾巴的翻译后修饰被认为是染色质向细胞发出的各种过程信号。本文展示的实验表明,多线染色体中组蛋白H3和H4的乙酰化在热休克期间不会改变。相反,热休克期间磷酸化H3的整体水平显著下降,同时在热休克位点观察到H3磷酸化增加。额外的实验证实,磷酸化H3分布的这种变化依赖于功能性热休克转录因子活性。这些实验表明,H3磷酸化在热休克反应期间的转录诱导中起重要作用。