Rel同源区域中存在非α-螺旋DNA结合基序的证据。

Liu J, Sodeoka M, Lane W S, Verdine G L

Department of Chemistry, Harvard University, Cambridge, MA 02138.

Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):908-12. doi: 10.1073/pnas.91.3.908.

The Rel family of transcription factors serve as terminal messengers in a variety of developmental and receptor-mediated signaling pathways. These proteins are related by a domain of approximately 280 amino acids, the Rel homology region, which mediates dimerization and sequence-specific binding to DNA. Here we report the use of photocrosslinking and site-directed mutagenesis to identify specific contact partners in a Rel protein-DNA interface. Within the Rel homology region of NF-kappa B p50 (also known as KBF1), two amino acid residues were identified by photocrosslinking to adjacent bases in a beta-interferon regulatory element. Secondary structure analysis suggests that the DNA-binding motif of the Rel homology region comprises a beta-turn-beta structure, in contrast to the alpha-helical motifs so commonly observed in transcription factors.

转录因子的Rel家族在多种发育和受体介导的信号通路中充当终端信使。这些蛋白质通过一个约280个氨基酸的结构域即Rel同源区相关联，该区域介导二聚化以及与DNA的序列特异性结合。在此我们报告利用光交联和定点诱变来鉴定Rel蛋白-DNA界面中的特定接触伙伴。在核因子-κB p50（也称为KBF1）的Rel同源区内，通过光交联鉴定出两个氨基酸残基，它们与β-干扰素调节元件中的相邻碱基相互作用。二级结构分析表明，Rel同源区的DNA结合基序包含一个β-转角-β结构，这与转录因子中常见的α-螺旋基序不同。