MTERF1

Mitochondrial transcription termination factor 1, also known as MTERF1, is a protein which in humans is encoded by the MTERF gene.[5][6][7][8]

MTERF1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMTERF1, MTERF, mitochondrial transcription termination factor 1
External IDsOMIM: 602318 MGI: 3704243 HomoloGene: 5073 GeneCards: MTERF1
Gene location (Human)
Chr.Chromosome 7 (human)[1]
Band7q21.2Start91,692,008 bp[1]
End91,880,702 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

7978

208595

Ensembl

ENSG00000127989

ENSMUSG00000053178

UniProt

Q99551

B9EJ57

RefSeq (mRNA)

NM_001301134
NM_001301135
NM_006980

NM_001042670

RefSeq (protein)

NP_001288063
NP_001288064
NP_008911

NP_001036135

Location (UCSC)Chr 7: 91.69 – 91.88 MbChr 5: 4.19 – 4.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

This gene encodes a mitochondrial transcription termination factor. This protein participates in attenuating transcription from the mitochondrial genome; this attenuation allows higher levels of expression of 16S ribosomal RNA relative to the tRNA gene downstream. The product of this gene has three leucine zipper motifs bracketed by two basic domains that are all required for DNA binding. There is evidence that, for this protein, the zippers participate in intramolecular interactions that establish the three-dimensional structure required for DNA binding.[5]

References

  1. GRCh38: Ensembl release 89: ENSG00000127989 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000053178 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: MTERF mitochondrial transcription termination factor".
  6. Daga A, Micol V, Hess D, Aebersold R, Attardi G (April 1993). "Molecular characterization of the transcription termination factor from human mitochondria". J. Biol. Chem. 268 (11): 8123–30. PMID 7681833.
  7. Asin-Cayuela J, Helm M, Attardi G (April 2004). "A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity". J. Biol. Chem. 279 (15): 15670–7. doi:10.1074/jbc.M312537200. PMID 14744862.
  8. Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM (July 2005). "The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form". J. Biol. Chem. 280 (27): 25499–505. doi:10.1074/jbc.M501145200. PMID 15899902.

Further reading


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