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酵母转录激活因子Ndt80的新型DNA结合结构域的晶体学研究。

Crystallographic studies of a novel DNA-binding domain from the yeast transcriptional activator Ndt80.

作者信息

Montano Sherwin P, Pierce Michael, Coté Marie L, Vershon Andrew K, Georgiadis Millie M

机构信息

Waksman Institute and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2127-30. doi: 10.1107/s0907444902015020. Epub 2002 Nov 23.

Abstract

The Ndt80 protein is a transcriptional activator that plays a key role in the progression of the meiotic divisions in the yeast Saccharomyces cerevisiae. Ndt80 is strongly induced during the middle stages of the sporulation pathway and binds specifically to a promoter element called the MSE to activate transcription of genes required for the meiotic divisions. Here, the preliminary structural and functional studies to characterize the DNA-binding activity of this protein are reported. Through deletion analysis and limited proteolysis studies of Ndt80, a novel 32 kDa DNA-binding domain that is sufficient for DNA-binding in vitro has been defined. Crystals of the DNA-binding domain of Ndt80 in two distinct lattices have been obtained, for which diffraction data extend to 2.3 A resolution.

摘要

Ndt80蛋白是一种转录激活因子,在酿酒酵母减数分裂进程中发挥关键作用。Ndt80在孢子形成途径的中期被强烈诱导,并特异性结合一种名为MSE的启动子元件,以激活减数分裂所需基因的转录。本文报道了表征该蛋白DNA结合活性的初步结构和功能研究。通过对Ndt80的缺失分析和有限蛋白酶解研究,确定了一个新的32 kDa DNA结合结构域,该结构域足以在体外结合DNA。已获得Ndt80 DNA结合结构域在两种不同晶格中的晶体,其衍射数据延伸至2.3 Å分辨率。

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