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.
Highlights
The human genome encodes approximately 290 Krüppel-associated box (KRAB) zinc finger proteins, but little is known about the biological functions of these proteins
To assess whether the zinc finger motifs of Zinc finger protein 133 (ZNF133) contribute to transcriptional repressor activity, we performed the GAL4 DNA-tethering assays (Oh et al, 2005; Kim et al, 2006)
To investigate whether histone deacetylase, which interacts with PIAS proteins (Tussie-Luna et al, 2002; Long et al, 2003; Gross et al, 2004), mediates the regulatory activity of protein inhibitor of activated STAT1 (PIAS1) on ZNF133, we investigated the effect of the HDAC inhibitor, trichostatin A (TSA), on this process
Summary
The human genome encodes approximately 290 Krüppel-associated box (KRAB) zinc finger proteins, but little is known about the biological functions of these proteins Proteins in this family are characterized by the presence of the KRAB domain near the amino termini and multiple zinc finger motifs (4 to 30) at their carboxy termini. TIF1β interacts with histone deacetylase complexes- NcoR1 (Underhill et al, 2000) and NuRD (Schultz et al, 2001) By associating with those proteins through the KRAB domain, KRAB zinc finger proteins are thought to exert transcriptional repressor activity on their targets, which are recognized by zinc finger motifs. Most zinc finger motifs are involved in DNA binding; some of the KRAB-zinc finger family proteins, including ZBRK1, have been shown to bind both DNA and protein via its zinc finger motifs (Zheng et al, 2000)
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