Masuda N, Yasumo H, Furusawa T, Tsukamoto T, Sadano H, Osumi T
Department of Life Science, Himeji Institute of Technology, Kamigori, Hyogo 678-1297, Japan.
Gene. 1998 Oct 23;221(2):225-33. doi: 10.1016/s0378-1119(98)00461-2.
To identify the proteins which may modulate the functions of peroxisome proliferator-activated receptor (PPAR), a rat liver cDNA library was screened by a yeast two-hybrid system, using the mouse PPARalpha as a bait. A protein named nuclear receptor binding factor-1 (NRBF-1) was identified, which interacts not only with PPARalpha, but also with various nuclear hormone receptors in the presence of the respective ligands. Both the hinge and ligand-binding domains of PPARalpha are required for the interaction. NRBF-1 seems to be translocated to the nucleus by a piggyback mechanism, together with PPARalpha. NRBF-1 has a significant homology to the yeast protein MRF1, a putative transcription factor regulating the expression of mitochondrial respiratory proteins. NRBF-1 might be another type of nuclear receptor co-operator.
为了鉴定可能调节过氧化物酶体增殖物激活受体(PPAR)功能的蛋白质,以小鼠PPARα为诱饵,通过酵母双杂交系统筛选大鼠肝脏cDNA文库。鉴定出一种名为核受体结合因子-1(NRBF-1)的蛋白质,它不仅与PPARα相互作用,而且在各自配体存在的情况下还与各种核激素受体相互作用。PPARα的铰链区和配体结合区对于这种相互作用都是必需的。NRBF-1似乎通过搭载机制与PPARα一起转运到细胞核中。NRBF-1与酵母蛋白MRF1具有显著同源性,MRF1是一种推测的调节线粒体呼吸蛋白表达的转录因子。NRBF-1可能是另一种类型的核受体辅调节因子。