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MTERF encodes a mitochondrial transcription termination factor. Additionally we are shipping Mitochondrial Transcription Termination Factor Antibodies (41) and Mitochondrial Transcription Termination Factor Kits (3) and many more products for this protein.
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mTerf5 knockdown led to enhanced replication pausing at mTTF binding sites, a decrease in fragile replication intermediates containing single-stranded segments, and the disappearance of species containing segments of RNA/DNA hybrid
The first ever-obtained evidence for an in vivo role of an animal mitochondrial transcription termination factor.
DmTTF might play multiple roles in the mtDNA transcription process, for which different levels of the protein with respect to mtRNApol are required.
MTERF1 has the ability to accommodate alternate active conformations.
It has been demonstrated that MTERF1 arrests mitochondrial DNA (mtDNA) replication with distinct polarity whereby MTERF1 acts as a directional contra-helicase, blocking mtDNA unwinding by the mitochondrial helicase TWINKLE.
Studies indicate that the structure of the mitochondrial transcription termination factor (MTERF1) provides insight into the mechanism of binding, recognition of the termination sequence and the conformational changes involved in mediating termination.
Single nucleotide polymorphism in MTERF gene is associated with epithelial ovarian cancer.
Data show that mTERF protein levels materially affect the amount of readthrough transcription on the antisense strand of mtDNA, whilst the effects on sense-strand transcripts are complex, and suggest the influence of compensatory mechanisms.
Presented are the crystal structures of human mitochondrial regulator MTERF, a transcription termination factor also implicated in replication pausing, in complex with double-stranded DNA oligonucleotides containing the tRNA(Leu)(UUR) gene sequence.
The structure indicates that upon sequence recognition MTERF1 unwinds the DNA molecule, promoting eversion of three nucleotides.
mTERF mRNA levels were higher in elite athletes compared with moderately active subjects
mTERF exists in mitochondria in two forms, an active monomer and an inactive large size complex
monomeric human mTERF is fully active in its non-phosphorylated form and that the protein does not require additional cellular factors to terminate mitochondrial transcription in vitro
MTERF1 does not regulate heavy-strand transcription, but rather acts to block transcription on the opposite strand of mtDNA to prevent transcription interference at the light-strand promoter.
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.
mitochondrial transcription termination factor
, Transcription termination factor, mitochondrial
, mitochondrial transcription termination factor 1
, transcription termination factor, mitochondrial