Bardwell V J, Treisman R
Imperial Cancer Research Fund Laboratories, London, UK.
Genes Dev. 1994 Jul 15;8(14):1664-77. doi: 10.1101/gad.8.14.1664.
We describe a novel zinc finger protein, ZID (zinc finger protein with interaction domain). At its amino terminus ZID contains a 120-amino-acid conserved motif present in a large family of proteins that includes both the otherwise unrelated zinc finger proteins, such as Ttk, GAGA, and ZF5, and a group of poxvirus proteins: We therefore refer to this domain as the POZ (poxvirus and zinc finger) domain. The POZ domains of ZID, Ttk, and GAGA act to inhibit the interaction of their associated finger regions with DNA. This inhibitory effect is not dependent on interactions with other proteins and does not appear dependent on specific interactions between the POZ domain and the finger region. The POZ domain acts as a specific protein-protein interaction domain: The POZ domains of ZID and Ttk can interact with themselves but not with each other, POZ domains from ZF5, or the viral protein SalF17R. However, the POZ domain of GAGA can interact efficiently with the POZ domain of Ttk. In transfection experiments, the ZID POZ domain inhibits DNA binding in NIH-3T3 cells and appears to localize the protein to discrete regions of the nucleus. We discuss the implications of multimerization for the function of POZ domain proteins.
我们描述了一种新型锌指蛋白ZID（具有相互作用结构域的锌指蛋白）。ZID在其氨基末端含有一个120个氨基酸的保守基序，该基序存在于一大类蛋白质中，这类蛋白质既包括原本不相关的锌指蛋白，如Ttk、GAGA和ZF5，也包括一组痘病毒蛋白：因此，我们将这个结构域称为POZ（痘病毒和锌指）结构域。ZID、Ttk和GAGA的POZ结构域可抑制其相关指状区域与DNA的相互作用。这种抑制作用不依赖于与其他蛋白质的相互作用，似乎也不依赖于POZ结构域与指状区域之间的特异性相互作用。POZ结构域作为一种特异性蛋白质-蛋白质相互作用结构域：ZID和Ttk的POZ结构域可自身相互作用，但不能相互作用，也不能与ZF5的POZ结构域或病毒蛋白SalF17R相互作用。然而，GAGA的POZ结构域可与Ttk的POZ结构域有效相互作用。在转染实验中，ZID的POZ结构域抑制NIH-3T3细胞中的DNA结合，并似乎将该蛋白定位到细胞核的离散区域。我们讨论了多聚化对POZ结构域蛋白功能的影响。
