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Gene Review

MTERF1  -  mitochondrial transcription termination...

Homo sapiens

Synonyms: MTERF, Mitochondrial transcription termination factor 1, Transcription termination factor 1, mitochondrial, mTERF, mTERF1
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Disease relevance of MTERF


High impact information on MTERF

  • In the present work, addition of mTERF to a HeLa cell mitochondrial lysate-based reaction mixture containing an artificial rDNA template did indeed specifically stimulate rDNA transcription [3].
  • The human mitochondrial transcription termination factor (mTERF) cDNA has been cloned and expressed in vitro, and two alternative precursors of the protein have been imported into isolated mitochondria and processed to the mature protein [4].
  • The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions [4].
  • The precursors contain a mitochondrial targeting sequence, and the mature mTERF (342 residues) exhibits three leucine zippers, of which one is bipartite, and two widely spaced basic domains [4].
  • The MELAS mutation occurs within the mtDNA binding site for a protein factor (mTERF) that promotes termination of transcription at the 16S rRNA/tRNA(LeuUUR) gene boundary [5].

Biological context of MTERF

  • The termination activity has a distinct polarity, and we observed complete transcription termination when the mTERF-binding site is oriented in a forward position relative the heavy strand promoter but only partial transcription termination when the binding site is in the reverse position [6].
  • 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 [6].
  • 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 [6].
  • These data suggest that mTERF functioning in vivo is regulated by phosphorylation [7].
  • Here we report that mTERF is the first protein having a role in mammalian mitochondrial gene expression that appears to be controlled by phosphorylation [7].

Anatomical context of MTERF


Associations of MTERF with chemical compounds

  • No permanganate reactivity was associated with the other regions of the D-loop, including CSB-2 and -3, and with the mTERF contact site [9].
  • Dimethyl sulfate footprinting allowed the detection of protein-DNA interactions within the rat analogues of the human binding sites for the transcription termination factor mTERF and for the transcription activating factor mt-TFA [9].

Regulatory relationships of MTERF

  • The expression of mTERFL is dramatically inhibited by the addition of serum in serum-starved cells while the mTERF is rather induced [10].

Other interactions of MTERF


Analytical, diagnostic and therapeutic context of MTERF


  1. A novel point mutation in the mitochondrial tRNA(Leu)(UUR) gene in a family with mitochondrial myopathy. Goto, Y., Tojo, M., Tohyama, J., Horai, S., Nonaka, I. Ann. Neurol. (1992) [Pubmed]
  2. New DNA-binding activity of rat mitochondrial transcription termination factor (mTERF). Prieto-Martín, A., Montoya, J., Martínez-Azorín, F. J. Biochem. (2004) [Pubmed]
  3. Termination factor-mediated DNA loop between termination and initiation sites drives mitochondrial rRNA synthesis. Martin, M., Cho, J., Cesare, A.J., Griffith, J.D., Attardi, G. Cell (2005) [Pubmed]
  4. The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions. Fernandez-Silva, P., Martinez-Azorin, F., Micol, V., Attardi, G. EMBO J. (1997) [Pubmed]
  5. MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts. Chomyn, A., Martinuzzi, A., Yoneda, M., Daga, A., Hurko, O., Johns, D., Lai, S.T., Nonaka, I., Angelini, C., Attardi, G. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  6. The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form. Asin-Cayuela, J., Schwend, T., Farge, G., Gustafsson, C.M. J. Biol. Chem. (2005) [Pubmed]
  7. Phosphorylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA. Prieto-Martín, A., Montoya, J., Martínez-Azorín, F. Nucleic Acids Res. (2004) [Pubmed]
  8. A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity. Asin-Cayuela, J., Helm, M., Attardi, G. J. Biol. Chem. (2004) [Pubmed]
  9. Identification by in Organello footprinting of protein contact sites and of single-stranded DNA sequences in the regulatory region of rat mitochondrial DNA. Protein binding sites and single-stranded DNA regions in isolated rat liver mitochondria. Cantatore, P., Daddabbo, L., Fracasso, F., Gadaleta, M.N. J. Biol. Chem. (1995) [Pubmed]
  10. Cloning and functional analysis of human mTERFL encoding a novel mitochondrial transcription termination factor-like protein. Chen, Y., Zhou, G., Yu, M., He, Y., Tang, W., Lai, J., He, J., Liu, W., Tan, D. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. The mitochondrial ribomotor hypothesis. Martínez-Azorín, F. IUBMB Life (2005) [Pubmed]
  12. Molecular characterization of the transcription termination factor from human mitochondria. Daga, A., Micol, V., Hess, D., Aebersold, R., Attardi, G. J. Biol. Chem. (1993) [Pubmed]
  13. MTERF3, the most conserved member of the mTERF-family, is a modular factor involved in mitochondrial protein synthesis. Roberti, M., Bruni, F., Loguercio Polosa, P., Manzari, C., Gadaleta, M.N., Cantatore, P. Biochim. Biophys. Acta (2006) [Pubmed]
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