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首页> 外文期刊>Molecular and Cellular Biology >The N-terminal 96 residues of MCM1, a regulator of cell type-specific genes in Saccharomyces cerevisiae, are sufficient for DNA binding, transcription activation, and interaction with alpha 1.
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The N-terminal 96 residues of MCM1, a regulator of cell type-specific genes in Saccharomyces cerevisiae, are sufficient for DNA binding, transcription activation, and interaction with alpha 1.

机译：MCM1的N末端96个残基是酿酒酵母中细胞类型特异性基因的调节子，足以与DNA结合，转录激活以及与alpha 1相互作用。

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摘要

MCM1 performs several functions necessary for its role in regulating cell type-specific gene expression in the yeast Saccharomyces cerevisiae: DNA binding, transcription activation, and interaction with coregulatory proteins such as alpha 1. We analyzed a set of MCM1 deletion derivatives using in vivo reporter gene assays and in vitro DNA-binding studies to determine which regions of MCM1 are important for its various activities. We also analyzed a set of LexA-MCM1 hybrids to examine the ability of different segments of MCM1 to activate transcription independent of MCM1's DNA-binding function. The first third of MCM1 [MCM1(1-96)], which includes an 80-residue segment homologous to the mammalian serum response factor, was sufficient for high-affinity DNA binding, for activation of reporter gene expression, and for interaction with alpha 1 in vitro and in vivo. However, the ability of MCM1(1-96) to activate transcription and to interact with alpha 1 was somewhat reduced compared with wild-type MCM1 [MCM1(1-286)]. Optimal interaction with alpha 1 required residues 99 to 117, in which 18 of 19 amino acids are acidic in character. Optimal transcription activation required a segment from residues 188 to 286, in which 50% of the amino acids are glutamine. Deletion of this segment from MCM1 reduced expression of reporter genes by about twofold. Moreover, LexA-MCM1 hybrids containing this segment were able to activate expression of reporter genes that rely on LexA binding sites as potential upstream activation sequences. Thus, glutamine-rich regions may contribute to the activation function of yeast transcription activators, as has been suggested for glutamine-rich mammalian proteins such as Sp1.
机译：MCM1执行其在调节酿酒酵母中细胞类型特异性基因表达中所必需的几种功能：DNA结合，转录激活以及与诸如α1的共调节蛋白的相互作用。我们使用体内报告基因分析了一组MCM1缺失衍生物基因检测和体外DNA结合研究，以确定MCM1的哪些区域对其各种活性至关重要。我们还分析了一套LexA-MCM1杂种，以检查MCM1的不同片段激活独立于MCM1的DNA结合功能的转录的能力。 MCM1的前三分之一[MCM1（1-96）]包含与哺乳动物血清反应因子同源的80个残基片段，足以实现高亲和力DNA结合，激活报道基因表达以及与alpha相互作用1体外和体内。但是，与野生型MCM1 [MCM1（1-286）]相比，MCM1（1-96）激活转录并与alpha 1相互作用的能力有所降低。与α1的最佳相互作用需要残基99至117，其中19个氨基酸中的18个具有酸性。最佳的转录激活需要一个残基188至286的片段，其中50％的氨基酸是谷氨酰胺。从MCM1中删除此段可将报道基因的表达降低约两倍。此外，包含该片段的LexA-MCM1杂种能够激活依赖LexA结合位点作为潜在上游激活序列的报告基因的表达。因此，富含谷氨酰胺的区域可能有助于酵母转录激活因子的激活功能，正如针对富含谷氨酰胺的哺乳动物蛋白（例如Sp1）所建议的那样。

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