PIAS1 通过锌指基序与 KRAB 锌指蛋白 ZNF133 相互作用，并调节其转录活性。

PIAS1 interacts with the KRAB zinc finger protein, ZNF133, via zinc finger motifs and regulates its transcriptional activity.

作者信息

Lee Sang-Jin, Lee Jae-Rin, Hahn Hwa-Sun, Kim Young-Hoon, Ahn Jin-Hyun, Bae Chang-Dae, Yang Jun-Mo, Hahn Myong-Joon

机构信息

Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.

出版信息

Exp Mol Med. 2007 Aug 31;39(4):450-7. doi: 10.1038/emm.2007.49.

DOI:10.1038/emm.2007.49

PMID:17934332

Abstract

Zinc finger protein 133 (ZNF133) is composed of a Krüppel-associated box (KRAB) domain and 14 contiguous zinc finger motifs. ZNF133 is regarded as a transcriptional repressor because the KRAB domain has potent repressor activity and the zinc finger motifs usually act in binding to DNA. However, we found that the zinc finger motifs of ZNF133 also possessed transcriptional repressor activity. By two-hybrid screening assay, we found that the zinc finger motifs of ZNF133 interacted with protein inhibitor of activated STAT1 (PIAS1). PIAS1 enhanced the transcriptional repression activity of ZNF133 through the zinc finger motifs. This effect of PIAS1 was relieved by an inhibitor of the histone deacetylases (HDACs). These results demonstrate that the transcriptional repressor activity of ZNF133 is regulated by both the KRAB domain and the zinc finger motifs, and that the repressive effect by zinc finger motifs is mediated by PIAS1.

摘要

锌指蛋白133（ZNF133）由一个与Krüppel相关的盒（KRAB）结构域和14个连续的锌指基序组成。ZNF133被认为是一种转录抑制因子，因为KRAB结构域具有强大的抑制活性，而锌指基序通常作用于与DNA结合。然而，我们发现ZNF133的锌指基序也具有转录抑制活性。通过双杂交筛选试验，我们发现ZNF133的锌指基序与活化STAT1的蛋白抑制剂（PIAS1）相互作用。PIAS1通过锌指基序增强了ZNF133的转录抑制活性。组蛋白脱乙酰酶（HDACs）抑制剂可消除PIAS1的这种作用。这些结果表明，ZNF133的转录抑制活性受KRAB结构域和锌指基序的调控，并且锌指基序的抑制作用由PIAS1介导。