Numoto M, Yokoro K, Koshi J
Research Institute for Radiation Biology and Medicine, Hiroshima University, 1-2-3 Kasumi, Hiroshima, Minami-ku, 734, Japan.
Biochem Biophys Res Commun. 1999 Mar 24;256(3):573-8. doi: 10.1006/bbrc.1999.0375.
ZF5, which we have cloned as a transcriptional repressor on the mouse c-myc promoter, has the POZ domain at the amino-terminus and the Kruppel-type zinc finger domain at the carboxy-terminus. In this report, we showed that ZF5 has two contradictory functions in transcription: activation of human immunodeficiency virus (HIV) promoter and repression of the HSV thymidine kinase (TK) promoter. The POZ domain contributed to the repressor activity, whereas the active function resulted from the DNA-binding ability of the zinc finger domain. We demonstrated that the POZ domain has a function mediating homomeric protein-protein interaction and this interaction requires the zinc finger domain. Furthermore, the POZ domain decreased the DNA-binding activity of the zinc finger domain. These results can provide evidence indicating the important interaction between the POZ and zinc finger domains.
ZF5是我们作为小鼠c-myc启动子上的转录抑制因子克隆出来的,它在氨基末端有POZ结构域,在羧基末端有Kruppel型锌指结构域。在本报告中,我们表明ZF5在转录中具有两种相互矛盾的功能:激活人类免疫缺陷病毒(HIV)启动子和抑制单纯疱疹病毒胸苷激酶(TK)启动子。POZ结构域有助于抑制活性,而活性功能则源于锌指结构域的DNA结合能力。我们证明POZ结构域具有介导同源蛋白-蛋白相互作用的功能,这种相互作用需要锌指结构域。此外,POZ结构域降低了锌指结构域的DNA结合活性。这些结果可以提供证据表明POZ结构域和锌指结构域之间存在重要的相互作用。