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Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo. 总被引:9,自引:0,他引:9
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Recent work has shown that the yeast histone H4 N-terminus, while not essential for viability, is required for repression of the silent mating loci and activation of GAL1 and PHO5 promoters. Because histone H3 shares many structural features with histone H4 and is intimately associated with H4 in the assembled nucleosome, we asked whether H3 has similar functions. While the basic N-terminal domain of H3 is found to be non-essential (deletion of residues 4-40 of this 135 amino acid protein allows viability), its removal has only a minor effect on mating. Surprisingly, both deletions (of residues 4-15) and acetylation site substitutions (at residues 9, 14 and 18) within the N-terminus of H3 allow hyperactivation of the GAL1 promoter as well as a number of other GAL4-regulated genes including GAL2, GAL7 and GAL10. To a limited extent glucose repression is also alleviated by H3 N-terminal deletions. Expression of another inducible promoter, PHO5, is shown to be relatively unaffected. We conclude that the H3 and H4 N-termini have different functions in both the repression of the silent mating loci and in the regulation of GAL1. 相似文献
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The human transcriptional repressor protein NAB1: expression and biological activity 总被引:4,自引:0,他引:4
Thiel G Kaufmann K Magin A Lietz M Bach K Cramer M 《Biochimica et biophysica acta》2000,1493(3):289-301
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酵母PHO2与PHO4蛋白的激活活性的分析及两者的相互作用 总被引:3,自引:3,他引:0
PHO2与PHO4是酵母PHO5基因的两个正调控因子,本文发现,PHO2与酵母转录因子GAL4的DNA结合功能域融合后就能激活报道基因lacZ的表达,其激活力受高低磷影响,表明PHO2蛋白上存在酸性转录激活区。PHO2蛋白上酸性氨基酸丰富的287-326肽段并非PHO2的激活区。在PHO2蛋白上230位Ser处于磷酸化状态2PHO2才有激活作用,表明了这一磷酸化位点可能与PHO2的转录激活能力有关 相似文献
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Identification of a portable repression domain and an E1A-responsive activation domain in Pax4: a possible role of Pax4 as a transcriptional repressor in the pancreas 总被引:4,自引:0,他引:4
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Fujitani Y Kajimoto Y Yasuda T Matsuoka TA Kaneto H Umayahara Y Fujita N Watada H Miyazaki JI Yamasaki Y Hori M 《Molecular and cellular biology》1999,19(12):8281-8291
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