Exp Mol Med.  2007 Aug;39(4):450-457.

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

Affiliations
  • 1Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea. mjhahn@yurim.skku.ac.kr
  • 2Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center, Seoul 135-710, Korea.

Abstract

Zinc finger protein 133 (ZNF133) is composed of a Kruppel-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.

Keyword

protein inhibitors of activated STAT; repressor proteins; transcription, genetic; zinc fingers; ZNF133 protein

MeSH Terms

Cell Line
DNA-Binding Proteins/*metabolism
Histone Deacetylases/antagonists & inhibitors/metabolism
Humans
Protein Binding
Protein Inhibitors of Activated STAT/*metabolism
Protein Structure, Tertiary
Repressor Proteins/*metabolism
Small Ubiquitin-Related Modifier Proteins/*metabolism
Transcription, Genetic
Two-Hybrid System Techniques
Zinc Fingers
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