ArticleNature2011
Structure of human mitochondrial RNA polymerase.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.
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Who cites it
115 citing papers in PubMed, 198 citations in OpenAlex.
- Ionomycin suppresses cancer cell growth by disrupting mitochondrial transcription.FEBS open bio · 2026Article
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026Review
- POLRMT overexpression increases mtDNA transcription without affecting steady-state mRNA levels.Life science alliance · 2025Article
- Structural basis for promoter recognition and transcription factor binding and release in human mitochondria.Molecular cell · 2025Article
- Insights into the translational activation mechanisms of the COX1 mRNA in yeast mitochondria.Journal of cell science · 2025Article
- DragonRNA: Generality of DNA-primed RNA-extension activities by DNA-directed RNA polymerases.Nucleic acids research · 2025Article
- Structural basis for substrate binding and selection by human mitochondrial RNA polymerase.Nature communications · 2024Article
- Sequence-specific dynamic DNA bending explains mitochondrial TFAM's dual role in DNA packaging and transcription initiation.Nature communications · 2024Article
- The initiation of mitochondrial DNA replication.Biochemical Society transactions · 2024Review
- The molecular machinery for maturation of primary mtDNA transcripts.Human molecular genetics · 2024Review
- Applications of Synthetic Pentatricopeptide Repeat Proteins.Plant & cell physiology · 2024Review
- Mechanisms and regulation of human mitochondrial transcription.Nature reviews. Molecular cell biology · 2024Review
- Assessing the Role of Post-Translational Modifications of Mitochondrial RNA Polymerase.International journal of molecular sciences · 2023Article
- Let's make it clear: systematic exploration of mitochondrial DNA- and RNA-protein complexes by complexome profiling.Nucleic acids research · 2023Article
- N-Acryloylindole-alkyne (NAIA) enables imaging and profiling new ligandable cysteines and oxidized thiols by chemoproteomics.Nature communications · 2023Article
- TEFM variants impair mitochondrial transcription causing childhood-onset neurological disease.Nature communications · 2023Article
- Mesoscale structure-function relationships in mitochondrial transcriptional condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Pet127 protein is a mitochondrial 5'-to-3' exoribonuclease from the PD-(D/E)XK superfamily involved in RNA maturation and intron degradation in yeasts.RNA (New York, N.Y.) · 2022Article
- The PPR domain of mitochondrial RNA polymerase is an exoribonuclease required for mtDNA replication in Drosophila melanogaster.Nature cell biology · 2022Article
55 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription of the mitochondrial genome is performed by a single-subunit RNA polymerase (mtRNAP) that is distantly related to the RNAP of bacteriophage T7, the pol I family of DNA polymerases, and single-subunit RNAPs from chloroplasts. Whereas T7 RNAP can initiate transcription by itself, mtRNAP requires the factors TFAM and TFB2M for binding and melting promoter DNA. TFAM is an abundant protein that binds and bends promoter DNA 15-40 base pairs upstream of the transcription start site, and stimulates the recruitment of mtRNAP and TFB2M to the promoter. TFB2M assists mtRNAP in promoter melting and reaches the active site of mtRNAP to interact with the first base pair of the RNA-DNA hybrid. Here we report the X-ray structure of human mtRNAP at 2.5 Å resolution, which reveals a T7-like catalytic carboxy-terminal domain, an amino-terminal domain that remotely resembles the T7 promoter-binding domain, a novel pentatricopeptide repeat domain, and a flexible N-terminal extension. The pentatricopeptide repeat domain sequesters an AT-rich recognition loop, which binds promoter DNA in T7 RNAP, probably explaining the need for TFAM during promoter binding. Consistent with this, substitution of a conserved arginine residue in the AT-rich recognition loop, or release of this loop by deletion of the N-terminal part of mtRNAP, had no effect on transcription. The fingers domain and the intercalating hairpin, which melts DNA in phage RNAPs, are repositioned, explaining the need for TFB2M during promoter melting. Our results provide a new venue for the mechanistic analysis of mitochondrial transcription. They also indicate how an early phage-like mtRNAP lost functions in promoter binding and melting, which were provided by initiation factors in trans during evolution, to enable mitochondrial gene regulation and the adaptation of mitochondrial function to changes in the environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.