ArticleMolecular and cellular biology2006
The zinc-sensing mechanism of mouse MTF-1 involves linker peptides between the zinc fingers.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 65 citations in OpenAlex.
- Conformational dynamics in specialized CProtein science : a publication of the Protein Society · 2025Article
- Emerging perspectives of copper-mediated transcriptional regulation in mammalian cell development.Metallomics : integrated biometal science · 2024Review
- Comparative cisplatin reactivity towards human Zn7-metallothionein-2 and MTF-1 zinc fingers: potential implications in anticancer drug resistance.Metallomics : integrated biometal science · 2022Article
- The Oxidative Balance Orchestrates the Main Keystones of the Functional Activity of Cardiomyocytes.Oxidative medicine and cellular longevity · 2022Review
- The classic metal-sensing transcription factor MTF1 promotes myogenesis in response to copper.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Cellular sensing and transport of metal ions: implications in micronutrient homeostasis.The Journal of nutritional biochemistry · 2015Review
- Regulation of intracellular Zn homeostasis in two intestinal epithelial cell models at various maturation time points.The journal of physiological sciences : JPS · 2015Article
- Inhibition of endogenous MTF-1 signaling in zebrafish embryos identifies novel roles for MTF-1 in development.Biochimica et biophysica acta · 2014Article
- Metal-responsive transcription factor 1 (MTF-1) activity is regulated by a nonconventional nuclear localization signal and a metal-responsive transactivation domain.Molecular and cellular biology · 2009Article
- Zinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1.PLoS pathogens · 2009Article
- Induction of metallothionein I by arsenic via metal-activated transcription factor 1: critical role of C-terminal cysteine residues in arsenic sensing.The Journal of biological chemistry · 2009Article
- Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations.Molecular and cellular biology · 2009Article
- Zinc-induced formation of a coactivator complex containing the zinc-sensing transcription factor MTF-1, p300/CBP, and Sp1.Molecular and cellular biology · 2008Article
- Copper sensing function of Drosophila metal-responsive transcription factor-1 is mediated by a tetranuclear Cu(I) cluster.Nucleic acids research · 2008Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
Mouse metal response element-binding transcription factor-1 (MTF-1) regulates the transcription of genes in response to a variety of stimuli, including exposure to zinc or cadmium, hypoxia, and oxidative stress. Each of these stresses may increase labile cellular zinc, leading to nuclear translocation, DNA binding, and transcriptional activation of metallothionein genes (MT genes) by MTF-1. Several lines of evidence suggest that the highly conserved six-zinc finger DNA-binding domain of MTF-1 also functions as a zinc-sensing domain. In this study, we investigated the potential role of the peptide linkers connecting the four N-terminal zinc fingers of MTF-1 in their zinc-sensing function. Each of these three linkers is unique, completely conserved among all known vertebrate MTF-1 orthologs, and different from the canonical Cys2His2 zinc finger TGEKP linker sequence. Replacing the RGEYT linker between zinc fingers 1 and 2 with TGEKP abolished the zinc-sensing function of MTF-1, resulting in constitutive DNA binding, nuclear translocation, and transcriptional activation of the MT-I gene. In contrast, swapping the TKEKP linker between fingers 2 and 3 with TGEKP had little effect on the metal-sensing functions of MTF-1, whereas swapping the canonical linker for the shorter TGKT linker between fingers 3 and 4 rendered MTF-1 less sensitive to zinc-dependent activation both in vivo and in vitro. These observations suggest a mechanism by which physiological concentrations of accessible cellular zinc affect MTF-1 activity. Zinc may modulate highly specific, linker-mediated zinc finger interactions in MTF-1, thus affecting its zinc- and DNA-binding activities, resulting in translocation to the nucleus and binding to the MT-I gene promoter.
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