...
首页> 外文期刊>Molecular and Cellular Biology >The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.
【24h】

The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.

机译:酵母调节蛋白ADR1以锌依赖性方式与ADH2的上游激活序列结合。

获取原文
   

获取外文期刊封面封底 >>

       

摘要

The yeast ADR1 protein contains two zinc finger domains that are essential for its role in transcriptional activation of alcohol dehydrogenase (ADH2). These domains are thought to function as DNA-binding structures. An ADR1-beta-galactosidase fusion protein made in Escherichia coli and containing the finger domains of ADR1 binds in vitro in a zinc-dependent manner to DNA fragments containing the two ADH2 upstream activation sequences. The strongest binding is to upstream activation sequence 1, a 22-base-pair palindrome.
机译:酵母ADR1蛋白包含两个锌指结构域,这对于其在酒精脱氢酶(ADH2)转录激活中的作用至关重要。这些结构域被认为起着DNA结合结构的作用。在大肠杆菌中生产并含有ADR1指状结构域的ADR1-β-半乳糖苷酶融合蛋白在体外以锌依赖性方式与含有两个ADH2上游激活序列的DNA片段结合。最强的结合是上游激活序列1,一个22个碱基对的回文。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号