Chilibeck Kaari A, Wu Tao, Liang Chao, Schellenberg Matthew J, Gesner Emily M, Lynch Jeffrey M, MacMillan Andrew M
Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
J Biol Chem. 2006 Jun 16;281(24):16530-5. doi: 10.1074/jbc.M511831200. Epub 2006 Apr 17.
Members of the ADAR (adenosine deaminase that acts on RNA) enzyme family catalyze the hydrolytic deamination of adenosine to inosine within double-stranded RNAs, a poorly understood process that is critical to mammalian development. We have performed fluorescence resonance energy transfer experiments in mammalian cells transfected with fluorophore-bearing ADAR1 and ADAR2 fusion proteins to investigate the relationship between these proteins. These studies conclusively demonstrate the homodimerization of ADAR1 and ADAR2 and also show that ADAR1 and ADAR2 form heterodimers in human cells. RNase treatment of cells expressing these fusion proteins changes their localization but does not affect dimerization. Taken together these results suggest that homo- and heterodimerization are important for the activity of ADAR family members in vivo and that these associations are RNA independent.
ADAR（作用于RNA的腺苷脱氨酶）酶家族成员催化双链RNA中腺苷向肌苷的水解脱氨反应，这一过程目前尚不清楚，但对哺乳动物发育至关重要。我们在转染了携带荧光团的ADAR1和ADAR2融合蛋白的哺乳动物细胞中进行了荧光共振能量转移实验，以研究这些蛋白之间的关系。这些研究确凿地证明了ADAR1和ADAR2的同二聚化，同时也表明ADAR1和ADAR2在人类细胞中形成异二聚体。对表达这些融合蛋白的细胞进行核糖核酸酶处理会改变它们的定位，但不影响二聚化。综合这些结果表明，同二聚化和异二聚化对ADAR家族成员在体内的活性很重要，并且这些结合是不依赖RNA的。
