Dorn A, Benoist C, Mathis D
Laboratoire de Génétique Moléculaire des Eucaryotes, Centre National de La Recherche Scientifique, Strasbourg, France.
Mol Cell Biol. 1989 Jan;9(1):312-20. doi: 10.1128/mcb.9.1.312-320.1989.
We report the discovery of a new B-lymphocyte-specific enhancer-binding protein. A series of gel retardation assays using fragments that scan the -2172 to -1180 region of the major histocompatibility complex class II gene E alpha reveal a site (W) that serves as the recognition sequence for two nuclear proteins, one B-cell restricted and the other ubiquitously occurring. Certain characteristics of the NF-W1 and NF-W2 pair recall the OTF-2/NF-A2 and OTF-1/NF-A1 pair that binds to the immunoglobulin octamer, but we demonstrate that the two protein pairs are distinguishable by several criteria. NF-W1 and NF-W2 interact differentially with their common GTTGCATC binding site, display a different affinity for it, and have molecular weights that differ by about 20,000. Yet, proteolysis experiments and cross-linking analyses indicate that the two W complexes show structural relatedness.
我们报告了一种新的B淋巴细胞特异性增强子结合蛋白的发现。使用扫描主要组织相容性复合体II类基因Eα的-2172至-1180区域的片段进行的一系列凝胶阻滞试验揭示了一个位点(W),它作为两种核蛋白的识别序列,一种是B细胞限制性的,另一种是普遍存在的。NF-W1和NF-W2对的某些特征使人联想到与免疫球蛋白八聚体结合的OTF-2/NF-A2和OTF-1/NF-A1对,但我们证明这两种蛋白对在几个标准上是可区分的。NF-W1和NF-W2与其共同的GTTGCATC结合位点有不同的相互作用,对其显示出不同的亲和力,并且分子量相差约20,000。然而,蛋白水解实验和交联分析表明,两种W复合物显示出结构相关性。