Abstract
MTF-1（metal-regulatory transcription factor-1）is a constitutively expressed protein that regulates metallothionein gene expression. The MTF-1 contains six zinc finger structures at the N-terminal region and an activation domain at C-terminus. In this work, we tried to express the His-tagged full length and truncated mMTF-1（pMTF-1）which contains six zinc fingers in E.coli expression system. We found that expressing of pMTF-1 at 16℃ improved the solubility of the protein. After eluting from nickel column, we used gel filtration to further purify the pMTF-1. We investigated the DNA binding activity of pMTF-1 by electrophoresis mobility shift assay. Notably, the DNA binding activity of pMTF-1 was absent after the purification. However the DNA binding activity recovered when incubating pMTF-1 with CHO K1 cell extracts. In conclusion, we develop the expression and purification system of pMTF-1.