The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form.

@article{AsinCayuela2005TheHM,
  title={The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form.},
  author={Jordi Asin-Cayuela and Thomas Schwend and G{\'e}raldine Farge and Claes M. Gustafsson},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 27},
  pages={25499-505}
}
The human mitochondrial transcription termination factor (mTERF) is a 39-kDa protein that terminates transcription at the 3'-end of the 16 S rRNA gene and thereby controls expression of the ribosomal transcription unit of mitochondrial DNA. The transcription termination activity of human mTERF has been notoriously difficult to study in vitro, and it has been suggested that the activity of the protein is regulated by posttranslational modifications or by protein polymerization. We here… CONTINUE READING