| First Author | Remondelli P | Year | 1997 |
| Journal | Biochem J | Volume | 323 ( Pt 1) |
| Pages | 79-85 | PubMed ID | 9173905 |
| Mgi Jnum | J:39506 | Mgi Id | MGI:86900 |
| Doi | 10.1042/bj3230079 | Citation | Remondelli P, et al. (1997) Interactions of the zinc-regulated factor (ZiRF1) with the mouse metallothionein Ia promoter. Biochem J 323(Pt 1):79-85 |
| abstractText | A mouse cDNA clone, M96, encoding a metal-regulating-element (MRE)-binding protein, was analysed for its ability to act as a metal-regulated transcription factor. The metal depletion of a glutathione S-transferase (GST)-M96 fusion protein showed that Zn2+ ions modulate the MRE-binding activity, suggesting that the M96-encoded protein is a Zn2+-regulated factor (ZiRF1). The methylation interference assay showed the specific interactions of ZiRF1 with the MRE, MREd/c, present on the mouse metallothionein Ia promoter. Point mutations of the MREd/c nullified the metal-regulatory properties of this region. In mouse L-cell nuclear extracts, mobility-shift assays revealed a Zn2+-dependent MRE-binding complex (MBC) with DNA-recognition properties similar to those of ZiRF1. Antibodies raised against purified GST-ZiRF1 were able to specifically recognize MBC in Western-blot analyses. Competition analysis of MRE-binding proteins from mouse NIH3T3 cells with oligonucleotide matching the binding sites for SP1 and MTF1 confirmed that both the basal SP1 and the metal-regulated MBC/ZiRF1 interact with the MREd/c region. The significance of mutual interactions with the metal-responsive promoter regions of either metal-regulated or basal transcription factors is discussed. |
