...
首页> 外文期刊>Molecular and Cellular Biology >Zinc fingers and other domains cooperate in binding of Drosophila sry beta and delta proteins at specific chromosomal sites.
【24h】

Zinc fingers and other domains cooperate in binding of Drosophila sry beta and delta proteins at specific chromosomal sites.

机译:锌指和其他域在特定的染色体位点上结合果蝇的β和δ蛋白。

获取原文
           

摘要

The closely related Drosophila serendipity (sry) beta and delta zinc finger proteins display consensus in vitro DNA recognition sequences differing by 4 of 13 nucleotide positions and bind in vivo to distinct sets of sites on polytene chromosomes. We compared the pattern of in vivo chromosomal binding of deleted forms of the sry delta protein fused to beta-galactosidase and expressed in Drosophila transgenic lines. Results show that the carboxy-terminal DNA-binding finger domain is required and sufficient for binding at specific chromosomal sites but that this binding does not nearly reproduce the wild-type pattern. An NH2-terminal domain of the sry delta protein is essential to its specificity of in vivo interaction with chromatin. In vitro and in vivo experiments using reciprocal finger swap between the sry beta and delta proteins suggest that the in vivo specificity is dependent on selective protein-protein contacts at defined chromosomal sites, in addition to DNA specific recognition.
机译:密切相关的果蝇偶然性(sry)β和δ锌指蛋白在13个核苷酸位置中有4个显示出一致的体外DNA识别序列,并在体内与多态染色体上不同的位点结合。我们比较了与β-半乳糖苷酶融合并在果蝇转基因株系中表达的缺失形式的sryδ蛋白的体内染色体结合模式。结果表明,羧基末端DNA结合指结构域是必需的,并且对于在特定染色体位点的结合是足够的,但是这种结合几乎不能复制野生型模式。 sryδ蛋白的NH2末端结构域对其在体内与染色质相互作用的特异性至关重要。使用sry beta蛋白和δ蛋白之间的相互手指互换的体外和体内实验表明,除了DNA特异性识别外,体内特异性还取决于在定义的染色体位点的选择性蛋白质-蛋白质接触。

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