Eklund E A, Lee S W, Skalnik D G
Herman B Wells Center for Pediatric Research, Department of Pediatrics, Indiana University School of Medicine, Indianapolis 46202, USA.
Gene. 1995 Apr 3;155(2):231-5. doi: 10.1016/0378-1119(94)00898-3.
We report the cloning of a human complementary DNA that encodes a protein which exhibits 36% identity and 62% similarity to Escherichia coli ribosomal protein S1 (rpS1), including conservation of four copies of an RNA-binding domain. This clone was obtained by ligand-screening a lambda gt11 expression library with a DNA probe derived from the CYBB gene promoter. Electrophoretic mobility shift and Southwestern blot assays confirm DNA binding activity of the protein, which exhibits preferential binding to single-stranded and double-stranded DNA and a low binding affinity for RNA. Hence, the rpS1 protein domain previously identified as an RNA-binding motif can also serve as a DNA-binding domain.
我们报道了一个人类互补DNA的克隆，该DNA编码一种蛋白质，该蛋白质与大肠杆菌核糖体蛋白S1（rpS1）具有36%的同一性和62%的相似性，包括四个RNA结合结构域拷贝的保守性。该克隆是通过用来自CYBB基因启动子的DNA探针筛选λgt11表达文库获得的。电泳迁移率变动分析和蛋白质印迹分析证实了该蛋白质的DNA结合活性，该蛋白质对单链和双链DNA表现出优先结合，对RNA的结合亲和力较低。因此，先前被鉴定为RNA结合基序的rpS1蛋白结构域也可作为DNA结合结构域。
