Klemsz M J, McKercher S R, Celada A, Van Beveren C, Maki R A
Cancer Research Center, La Jolla Cancer Research Foundation, California 92037.
Cell. 1990 Apr 6;61(1):113-24. doi: 10.1016/0092-8674(90)90219-5.
We have isolated a cDNA clone, PU.1, that codes for a new tissue-specific DNA binding protein. Analysis of the binding site by methylation interference and DNAase 1 protection revealed that the PU.1 protein recognized a purine-rich sequence, 5'-GAGGAA-3' (PU box). The PU.1 protein was shown to be a transcriptional activator that is expressed in macrophages and B cells. cDNA constructions used to generate proteins lacking portions of either the amino- or carboxy-terminal ends of the PU.1 protein placed the DNA binding domain in the highly basic carboxy-terminal domain of the protein. The amino acid sequence in the binding domain of PU.1 has considerable identity with proteins belonging to the ets oncogene family.
我们分离出了一个cDNA克隆，即PU.1，它编码一种新的组织特异性DNA结合蛋白。通过甲基化干扰和DNA酶I保护对结合位点进行分析，结果显示PU.1蛋白识别一个富含嘌呤的序列5'-GAGGAA-3'（PU盒）。已证明PU.1蛋白是一种在巨噬细胞和B细胞中表达的转录激活因子。用于生成缺失PU.1蛋白氨基端或羧基端部分的蛋白质的cDNA构建体，将DNA结合结构域置于该蛋白高度碱性的羧基端结构域中。PU.1结合结构域中的氨基酸序列与ets癌基因家族的蛋白质有相当高的同源性。
