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首页> 外文期刊>Molecular and Cellular Biology >Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors.
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Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptors.

机译：酵母RSP5及其人类同源物hRPF1增强了人类孕激素和糖皮质激素受体的激素依赖性转录激活。

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We have developed a system in Saccharomyces cerevisiae in which agonist-dependent transcriptional activity of the human progesterone receptor (hPR) is elevated to the point that it compromises cell growth. Screens for suppressors of this phenotype led to the demonstration that RSP5 is involved in hPR transactivation. Expression of RSP5 in yeast cells potentiated hPR and human glucocorticoid receptor (hGR) transcriptional activity and increased the efficacy of weak agonists of these receptors. Remarkably, expression of this yeast protein in mammalian cells had a similar effect on PR and GR transcriptional activity. Importantly, a human homolog of RSP5, hRPF1, functioned identically in mammalian cells. Previously, it has been demonstrated that RSP5 overexpression in yeast cells suppressed mutations within SPT3, a protein which interacts with the TATA-box-binding protein (TBP), suggesting that RSP5 and SPT3 operate in the same regulatory pathway. In support of this observation, we have shown that SPT3 enhances the activity of RSP5 on GR and PR when tested in yeast or mammalian cells. We conclude from these experiments that the regulatory pathways in which RSP5 and SPT3 operate in yeast cells are conserved in higher eukaryotes. Additionally, since SPT3 has been shown to contact yeast TBP directly and is the likely homolog of human TBP-associated factor TAFII18, we propose that RSP5/hRPF1 and SPT3 establish a functional link between activated PR and GR and the general transcription apparatus.
机译：我们已经开发了酿酒酵母中的系统，其中人孕激素受体（hPR）的激动剂依赖性转录活性被提高到损害细胞生长的程度。筛选这种表型的抑制剂导致证明RSP5参与hPR反式激活。 RSP5在酵母细胞中的表达增强了hPR和人类糖皮质激素受体（hGR）的转录活性，并增强了这些受体的弱激动剂的功效。值得注意的是，该酵母蛋白在哺乳动物细胞中的表达对PR和GR转录活性具有相似的作用。重要的是，RSP5的人类同源物hRPF1在哺乳动物细胞中的功能相同。以前，已经证明酵母细胞中RSP5的过表达抑制了SPT3（一种与TATA盒结合蛋白（TBP）相互作用）的蛋白中的突变，这表明RSP5和SPT3以相同的调节途径起作用。为了支持该观察，我们已经表明，当在酵母或哺乳动物细胞中测试时，SPT3增强RSP5对GR和PR的活性。我们从这些实验中得出结论，RSP5和SPT3在酵母细胞中起作用的调控途径在高等真核生物中是保守的。此外，由于已显示SPT3直接接触酵母TBP，并且可能是人TBP相关因子TAFII18的同源物，因此我们建议RSP5 / hRPF1和SPT3在激活的PR和GR与一般转录装置之间建立功能性联系。

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