Abstract
Metal-responsive transcription factor (MTF-1) regulate the gene related to metal homeostasis, which translocate to nucleus when heavy metal treatment. Previous studies indicated that As induced the interaction between MTF-1 and PML. In our experiment show that PML increase the protein expression of MTF-1 in the HEK293 cell, but does not alter the transcription of MTF-1 mRNA. The PML isoforms, PMLI to PMLVI cause MTF-1 protein accumulation without regulating MTF-1 protein stability. We found that the N-terminal including Zinc finger domain of MTF-1 accumulated by PML, and the deletion of MTF-1 NLS does not affect MTF-1 protein accumulation. Furthermore, the deletion of PML NLS would not affect MTF-1 protein accumulation, showing that MTF-1 is not a regulated protein of PML-NB. Finally, although we found that PML increases MTF-1 protein accumulation, but it does not alter the expression of MT2A, suggesting the increased MTF-1 caused by PML is not functional in the transcriptional level.