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the frequency of variation in sequence identity and length at conserved sequence block 2 amongst human mitochondrial genomes and used in vitro transcription to assess the effects of this length heterogeneity on the activity of the mitochondrial RNA polymerase, POLRMT, was examined.
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Suggest targeting POLRMT as strategy for treating acute myeloid leukemia.
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knock-down of MRPL12 by RNA interference results in instability of POLRMT.
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Results show that polymorphisms at POLG2 and POLRMT increased risk of oral cancer and leukoplakia, respectively, probably modulating synthesis and activity of the enzymes.
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The results reveal the organization of TFAM, POLRMT and TFB2M around the light-strand promoter and represent the first structural characterization of the entire mitochondrial transcriptional initiation complex.
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The results demonstrate that human TFAM binds to the N-terminal domain of mtRNAP, which results in bending of the promoter DNA around mtRNAP.
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Newly synthesized RNA exits toward the pentatricopeptide repeat (PPR) domain, a unique feature of mtRNAP with conserved RNA-recognition motifs.
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Authors propose that POLRMT interacts directly with h-mtTFB1 in 28S mitochondrial ribosomes to augment its 12S rRNA methyltransferase activity.
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X-ray structure of human mtRNAP at 2.5 A resolution, which reveals a T7-like catalytic carboxy-terminal domain, an amino-terminal domain resembling the T7 promoter-binding domain, a novel pentatricopeptide repeat domain, and flexible N-terminal extension
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muscle actin genes are transcribed by nuclear isoform of mitochondrial RNA polymerase (spRNAP-IV) whereas the non-muscle actin genes are transcribed by the conventional RNA polymerase II (PolII)
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Human mitochondrial RNA polymerase: evaluation of the single-nucleotide-addition cycle on synthetic RNA/DNA scaffolds
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POLRMT can function as an origin-specific primase in mammalian mitochondria.
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human mitochondrial DNA polymerase has a role in autosomal dominant progressive external ophthalmoplegia
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POLRMT recognizes promoter elements in a sequence specific manner; TFAM induces a structural change of the promoter that is required for POLRMT-dependent promoter recognition
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transcription of some mRNAs in humans and rodents is mediated by a previously unknown single-polypeptide nuclear RNA polymerase (spRNAP-IV), expressed from an alternative transcript of the mitochondrial RNA polymerase gene POLRMT
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the MRPL12 interaction with POLRMT is likely part of a novel regulatory mechanism that coordinates mitochondrial transcription with translation
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Promoter-independent DNA conformation-dependent transcription required TFB2M and was suppressed by TFAM, while promoter-dependent transcription was inhibited to a lesser extent BY TFAM.