Structural basis of mitochondrial transcription
Open accessAbstract
The mitochondrial genome is transcribed by a single-subunit DNA-dependent RNA polymerase (mtRNAP) and its auxiliary factors. Structural studies have elucidated how mtRNAP cooperates with its dedicated transcription factors to direct RNA synthesis: initiation factors TFAM and TFB2M assist in promoter-DNA binding and opening by mtRNAP while the elongation factor TEFM increases polymerase processivity to the levels required for synthesis of long polycistronic mtRNA transcripts. Here, we review the emerging body of structural and functional studies of human mitochondrial transcription, provide a molecular movie that can be used for teaching purposes and discuss the open questions to guide future directions of investigation.
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TFAM is essential for mtDNA genome maintenance and initiates mitochondrial transcription by recruiting POLRMT and TFB2M to specific promoter regions on mtDNA.
“TFAM is essential for mtDNA genome maintenance and initiates mitochondrial transcription by recruiting mitochondrial RNA polymerase (POLRMT) and mitochondrial transcription factor B (TFBM) to specific promoter regions on mtDNA (Hillen et al, 2017; Hillen et al, 2018).”
From The mitochondrial long non-coding RNA lncMtloop regulates mitochondrial transcription and suppresses Alzheimer’s disease (2024) · cites this paper as Hillen et al, 2018
The “Initiation factor TFAM” section (page unavailable) says TFAM binds promoter sites and recruits mitochondrial RNA polymerase to form a pre-initiation complex; TFB2M binds afterward to facilitate DNA opening. It also says TFAM is thought to mediate mitochondrial-genome packaging, but does not establish that TFAM is essential for genome maintenance or that it recruits TFB2M. (LLM, conf=0.86)
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Organization and regulation of gene transcription
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Self-citationMechanisms and regulation of protein synthesis in mitochondria
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“It may indicate that the polymerase-based transcription system was incorporated in eukaryotes early in the evolutionary process or that the proteobacterial system was replaced by phages in the process of evolution [84].”
BackgroundInfluentialStructure, mechanism, and regulation of mitochondrial DNA transcription initiation
Basu, U., Bostwick, A. M., Das, K., Dittenhafer‐Reed, K. E., & Patel, S. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011202 · Cited by 114 · see citing works
Mechanisms and regulation of human mitochondrial transcription
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“The eukaryotic nuclear RNAPs–RNAP I, II, and III–are multi-subunit RNAPs closely related in sequence and structure to bacterial RNAP (Cramer, 2002; Darst, 2001; Ebright, 2000; Werner and Grohmann, 2011); in contrast, mtRNAPs are single-subunit RNAPs that are unrelated in sequence and structure to multi-subunit RNAPs a…”
BackgroundSelf-citationMitochondrial Gene Expression and Beyond—Novel Aspects of Cellular Physiology
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“The NCR plays an important role as a site of H-strand synthesis initiation [49,54]; moreover, transcription initiation start sites for both mtDNA strands (ITL, light-strand transcription initiation site, ITH, heavy-strand transcription initiation site) are also located within the NCR.”
BackgroundInfluentialHuman Mitochondrial RNA Processing and Modifications: Overview
Jedynak-Slyvka, M., Jabczynska, A., & Szczęsny, R. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157999 · Cited by 71 · see citing works
“Structural studies have provided the precise mechanism of mitochondrial transcription initiation [17,18].”
BackgroundNon-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization
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POLRMT mutations impair mitochondrial transcription causing neurological disease
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Mesoscale structure–function relationships in mitochondrial transcriptional condensates
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Self-citationPhase separation drives the self-assembly of mitochondrial nucleoids for transcriptional modulation
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Mitochondria transcription and cancer
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“…machinery, consisting of mitochondrial RNA polymerase (POLRMT) and several transcription factors, including mitochondrial transcription factor A (TFAM), mitochondrial elongation factor (TEFM), mitochondrial transcription factor B2 (TFB2M) and mitochondrial termination factor (MTERF) [7].”
BackgroundZhou, X., Trinh‐Minh, T., Manh, C. T., Gießl, A., Bergmann, C., Györfi, A., Schett, G. A., & Distler, J. H. W. (2021) · Arthritis & Rheumatology · doi:10.1002/art.42033 · Cited by 45 · see citing works
“TFAM is encoded by the nuclear genome and thereby serves as a gatekeeper of the nuclear genome for mitochondrial fate (22).”
BackgroundPGC‐1α protects from myocardial ischaemia‐reperfusion injury by regulating mitonuclear communication
Li, Y., Jiao, Y., Liu, Y., Fu, J., Sun, L., & Su, J. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16236 · Cited by 38 · see citing works
Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix
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Starting the engine of the powerhouse: mitochondrial transcription and beyond
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Metabolic resistance to the inhibition of mitochondrial transcription revealed by CRISPR‐Cas9 screen
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Mitochondrial medicine: “from bench to bedside” 3PM-guided concept
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“…which is regulated by mitochondrial transcriptional complex that includes transcription factors POLRMT (mitochondrial RNA polymerase), TFB2M (mitochondrial transcription factor B2), and TFAM [121, 122], and known nuclear gene expression regulatory factors NRF-1/2, PRC, PGC1-β, and PGC1-α.”
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Mitochondrial RNA , a new trigger of the innate immune system
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“The mode of action of these proteins is more and more known (Hillen et al., 2018).”
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“The mitochondrial transcription machinery appears to be simple, composed of a monomeric RNA polymerase, POLRMT and only a few known co-factors: TFAM, TFB2M and TEFM (2,15).”
BackgroundInfluentialBiomolecular condensates and disease pathogenesis
Ruan, K., Bai, G., Fang, Y., Li, D., Li, T., Liu, X., Lu, B., Lü, Q., Songyang, Z., Sun, S., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2661-3 · Cited by 27 · see citing works
“Compared to nuclei, mitochondria have their own specific machineries for DNA transcription (Hillen et al., 2018).”
Function moves biomolecular condensates in phase space
Feric, M., & Misteli, T. (2022) · BioEssays · doi:10.1002/bies.202200001 · Cited by 26 · see citing works
“TFs, TFAM, and TFB2M, that recognize mt-promoters on template DNA.[60] Each of these components is capable of de-mixing from solution on its own, and when combined in vitro, they form viscoelastic condensates.”
BackgroundInfluentialMishra, P., Bhargava, A., Kumari, R., Bunkar, N., Chauhan, P., Mukherjee, S., Shandilya, R., Singh, R., Tiwari, R., & Chaudhury, K. (2022) · Atmospheric pollution research · doi:10.1016/j.apr.2022.101399 · Cited by 23 · see citing works
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“This observation is also strengthened by the increased expression of COX IV, Cyt C and of the transcription factor TFAM, which has a critical role in the initiation of mitochondrial transcription [26].”
BackgroundNo role for nuclear transcription regulators in mammalian mitochondria?
Rubalcava-Gracia, D., García-Villegas, R., & Larsson, N. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.010 · Cited by 25 · see citing works
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“TFAM binds nonspecifically to mtDNA, causing the DNA to bend and allowing the packaging of genetic material into nucleoids [9,45].”
BackgroundInfluentialCryo-EM Structures Reveal Transcription Initiation Steps by Yeast Mitochondrial RNA Polymerase
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Quality control of mitochondrial nucleoids
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Structures illustrate step-by-step mitochondrial transcription initiation
Goovaerts, Q., Shen, J., De Wijngaert, B., Basu, U., Patel, S. S., & Das, K. (2023) · Nature · doi:10.1038/s41586-023-06643-y · Cited by 16 · see citing works
“The Mtf1 hairpin homologue lever loop/B2 hairpin in h-mtRNAP supports TFB2M binding 1,2 .”
BackgroundInfluentialXiong, W., Xu, K., Sun, J. K.-L., Liu, S., Zhao, B., Shi, J., Herrup, K., Chow, H.-M., Lu, L., & Li, J. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00270-7 · Cited by 17 · see citing works
“TFAM is essential for mtDNA genome maintenance and initiates mitochondrial transcription by recruiting mitochondrial RNA polymerase (POLRMT) and mitochondrial transcription factor B (TFBM) to speci fi c promoter regions on mtDNA (Hillen et al, 2017; Hillen et al, 2018).”
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Noncanonical metabolite RNA caps: Classification, quantification, (de)capping, and function
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“The structurally similar, though unrelated, single-subunit RNA pols from mitochondria and some viruses like phage T7 (Hillen et al., 2018; Sousa, 1996) are apparently better adapted to NCIN incorporation than are the bacterial and nuclear RNA pols that belong to the multisubunit group (Ebright, 2000; Werner & Grohmann…”
BackgroundKnown types of membrane-less organelles and biomolecular condensates
Darling, A. L., & Uversky, V. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00002-6 · Cited by 15 · see citing works
Oxazinomycin arrests RNA polymerase at the polythymidine sequences
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“POLRMT has been reported to be responsible for catalyzing the transcription of the mitochondrial genome that encodes the essential 13 mtDNA-encoded OXPHOS protein subunits [52].”
BackgroundOkamoto, M., Shimogishi, M., Nakamura, A., Suga, Y., Sugawara, K., Sato, M., Nishi, R., Fujisawa, A., Yamamoto, Y., & Kashiba, M. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108988 · Cited by 14 · see citing works
The molecular machinery for maturation of primary mtDNA transcripts
Vučković, A., Freyer, C., Wredenberg, A., & Hillen, H. S. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae023 · Cited by 14 · see citing works
Self-citationLiu, L., Shao, M., Huang, Y., Qian, P., & Huang, H. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01615-9 · Cited by 14 · see citing works
“By cleaving tRNAs dispersed between mRNAs and rRNAs in precursors, 11 types of functional mRNAs are released [73, 74].”
BackgroundNever a dull enzyme, RNA polymerase II
Huang, J. S., & Ji, X. (2023) · Transcription · doi:10.1080/21541264.2023.2208023 · Cited by 13 · see citing works
“While mitochondrial RNA polymerases comprise a single protein [10,11], bacterial, archaeal, and eukaryotic RNA polymerases are considered holoenzymes vital for cell survival [4,13,14].”
BackgroundReview of 40 genes causing congenital myasthenic syndromes
Ohno, K., Ito, M., & Ohkawara, B. (2025) · Journal of Human Genetics · doi:10.1038/s10038-025-01355-9 · Cited by 12 · see citing works
Hepatic micropeptide modulates mitochondrial RNA processing machinery in hepatocellular carcinoma
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Identification of TEFM as a potential therapeutic target for LUAD treatment
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“Mitochondrial transcription factor B1 (TFB1M) is a critical nuclear-encoded factor that regulates mitochondrial transcription (Hillen et al. 2018).”
BackgroundDisruption of mitochondrial DNA integrity in cardiomyocyte injury upon ischemia/reperfusion
Hu, S., Tang, X., Zhu, F., Chen, L., Wang, S., Wang, H., Li, P., & Li, Y. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101282 · Cited by 7 · see citing works
“15,40 TFAM is a known mtDNA transcription factor.”
Qin, J., Shan, Y., Liu, H., Xue, Z., Xie, Y., Yuan, G., Zou, Y., Hao, X., Zhu, Y., Shen, X., et al. (2025) · Molecular Plant · doi:10.1016/j.molp.2025.03.018 · Cited by 7 · see citing works
High expression of the TEFM gene predicts poor prognosis in hepatocellular carcinoma
Fei, Z., Wang, W.-S., Li, S., Zi, J., Li, Y., Liu, T., Ao, S., Liu, Q., Cui, Q., Yu, M., et al. (2020) · Journal of Gastrointestinal Oncology · doi:10.21037/jgo-20-120 · Cited by 7 · see citing works
“Recombinant TEFM protein strongly promotes mitochondrial RNA polymerase (POLRMT) processivity as it stimulates the formation of longer transcripts in vitro (12).”
BackgroundPlazzi, F., Cras, Y. L., Formaggioni, A., & Passamonti, M. (2023) · Heredity · doi:10.1038/s41437-023-00650-5 · Cited by 7 · see citing works
“For example, since mitochondrial DNA is normally transcribed as a single polycistron (e.g., Hillen et al. 2018), structural signals ought to be present to cleave single transcripts, which are normally found between protein-coding genes as tRNA genes or short noncoding regions with stem-and-loop…”
Potter, A., Cabrera-Orefice, A., & Spelbrink, J. N. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad697 · Cited by 6 · see citing works
Exploring the microRNA-mitochondrial nexus in hepatocellular carcinoma
Akki, A. J., Nanduri, S., Patil, S. V., Das, K. K., & Parvatikar, P. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102045 · Cited by 6 · see citing works
Herbine, K., Nayak, A. R., Zamudio‐Ochoa, A., & Temiakov, D. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.06.016 · Cited by 6 · see citing works
Self-citationXu, Z., Mo, Y., Li, X., Hong, W., Shao, S., Liu, Y., Shu, F., Jiang, L., & Tan, N. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.773381 · Cited by 6 · see citing works
“Mterf1 can bind at this site, which can significantly reduce the affinity of RNA polymerase for the transcription template and terminate H-strand transcription in advance (Martin et al., 2005; AsinCayuela and Gustafsson, 2007; Terzioglu et al., 2013; Falkenberg, 2018; Hillen et al., 2018).”
BackgroundZhou, S., Ze, X., Feng, D., Liu, L., Shi, Y., Yu, M., Huang, L., Wang, Y., Men, H., Wu, J., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01178 · Cited by 6 · see citing works
Mitochondrial RNA metabolism, a potential therapeutic target for mitochondria-related diseases
Duan, T., Sun, L., Ding, K., Zhao, Q., Xu, L., Liu, C., & Sun, L. (2025) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003516 · Cited by 5 · see citing works
“[13] In addition, TEFM also enhances the transcriptional capacity of POLRMT by reducing the frequency and shortening the duration of long-lived pauses.”
Human mitochondrial RNA polymerase structures reveal transcription start site and slippage mechanism
Shen, J., Goovaerts, Q., Ajjugal, Y., De Wijngaert, B., Das, K., & Patel, S. S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.07.002 · Cited by 5 · see citing works
Cytosine methylase and hydroxymethylase activity in mammalian mitochondria
Shock, L. S., Thakkar, P. V., Robinson, J. M., & Taylor, S. M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1677402 · Cited by 5 · see citing works
“…executed by a three-component transcription initiation complex, comprised of a single-subunit DNA-directed RNA polymerase mitochondrial (POLRMT), and its auxiliary factors TFAM and mitochondrial transcription factor B2 (TFB2M) (Ramachandran et al., 2017; Morozov et al., 2015; Hillen et al., 2018).”
Cellular and viral RNA polymerases: evolutionary insights into eukaryotic origins
Wong, K. Y., Feng, X., Wang, X., Ji, X., & Zhou, Z. (2025) · Trends in Microbiology · doi:10.1016/j.tim.2025.11.008 · Cited by 5 · see citing works
Gupta, A., Shrivastava, D., Shakya, A. K., Gupta, K., Pratap, J., & Habib, S. (2020) · International Journal of Parasitology · doi:10.1016/j.ijpara.2020.07.010 · Cited by 5 · see citing works
Discovery, Processing, and Potential Role of Noncanonical Caps in RNA
Hu, H., Flynn, N., & Chen, X. (2021) · RNA technologies · doi:10.1007/978-3-030-71612-7_17 · Cited by 5 · see citing works
Li, L., Goel, A., & Wang, X. (2022) · Cell Biology and Toxicology · doi:10.1007/s10565-022-09721-5 · Cited by 5 · see citing works
Multi-phase separation in mitochondrial nucleoids and eukaryotic nuclei
Long, Q., Zhou, Y., Guo, J., Wu, H., & Liu, X. (2023) · Biophysics Reports · doi:10.52601/bpr.2023.220018 · Cited by 5 · see citing works
“Mitochondria have a series of special machinery in DNA replication and transcription, different from nuclear DNA replication and transcription (Hillen et al. 2018).”
BackgroundPOLRMT overexpression increases mtDNA transcription without affecting steady-state mRNA levels
Miranda, M., Mesaros, A., Scrima, N., Pérard, L., Kuznetsova, I., Purrio, M., Atanassov, I., Filipovska, A., Mourier, A., Larsson, N., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202302563 · Cited by 4 · see citing works
“…as atomic structures of transcription protein complexes (Wanrooij et al, 2008; Schwinghammer et al, 2013; Morozov et al, 2015; Posse et al, 2015; Hillen et al, 2018; Herbine et al, 2025) and several conditional knockout mouse models (Larsson et al, 1998; Kühl et al, 2016; Matic et al, 2018;…”
Xu, L., Zhang, T., Zhu, B., Tao, H., Liu, Y., Liu, X., Zhang, Y., & Meng, X. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101146 · Cited by 4 · see citing works
“Mitochondrial transcription factor A (TFAM), synthesized from nuclear DNA, is essential for transcribing 13 key enzymes encoded by the mitochondrial genome, vital for ETC assembly [69].”
Tissue specificity of energy metabolism in mitochondria
Moreno‐Loshuertos, R., & Fernández‐Silva, P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819621-2.00001-2 · Cited by 4 · see citing works
Mitochondrial Gene Expression of Three Different Dragonflies Under the Stress of Chlorpyrifos
Chen, Y., Yang, Z., Guo, Z., Zhan, L., Storey, K. B., Yu, D., & Zhang, J. (2025) · Insects · doi:10.3390/insects16010085 · Cited by 3 · see citing works
“…have been sequenced (providing important sequence information), data have also been gathered on other aspects of mitochondrial genes, including replication strategies [19,20], transcriptional and translational architectures [21,22], mutational information [23–25], and arrangements [26–30].”
He, X., Zhang, H., Wang, Y., Yan, H., Chen, Q., Su, M., Shi, Q., Zeng, X., Sheng, W., Wang, Y., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-025-3041-4 · Cited by 3 · see citing works
“Furthermore, Tfam and Tfb2m , two key transcription factors governing mitochondrial transcription (Hillen et al., 2018), were markedly upregulated in Aged-Defective oocytes (Figure 2F and G), suggesting that the elevation of mtRNA expression was likely driven by enhanced transcriptional activity of…”
TFAM in mtDNA Homeostasis: Open Questions
ALEXEYEV, M. F. (2023) · DNA · doi:10.3390/dna3030011 · Cited by 3 · see citing works
Structure-function relationships in mitochondrial transcriptional condensatesPreprint
Feric, M., Sarfallah, A., Dar, F., Temiakov, D., Pappu, R. V., & Misteli, T. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.30.474545 · Cited by 3 · see citing works
Self-citationXu, C., Wu, Y., Yang, S., Zhao, X., Zhang, H., Yan, Y., Zhao, J., Wei, W., Meng, Q., Wang, Y., et al. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111765 · Cited by 2 · see citing works
Epigenetic Threads of Neurodegeneration: TFAM’s Intricate Role in Mitochondrial Transcription
M, A. B. H., Prabhakaran, P., Logesh, R., Beeraka, N. M., Mathew, B., & Ravanappa, P. K. B. (2025) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273334342250108043032 · Cited by 2 · see citing works
The Central FacilitaTOR: Coordinating Transcription and Translation in Eukaryotes
Adams-Brown, S. E., & Reid, K. Z. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26072845 · Cited by 2 · see citing works
“TFAM, the mammalian ortholog of Hmo1, is mainly characterized as a component of the mitochondrial transcription initiation complex, which has its own polymerase, mtRNAP or POLRMT [208,209].”
High-Throughput Measurement of Mitochondrial RNA Turnover in Human Cultured Cells
Kotrys, A. V., Borowski, L. S., & Szczęsny, R. J. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0834-0_11 · Cited by 2 · see citing works
McElhenney, S. J., & Yu, J. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01568 · Cited by 2 · see citing works
“1,9,10,15 34 In T7 RNAP, both the PPi release and translocation have been studied via the all-atom MD and MSM construction.”
Mitochondrial DNA homeostasis: A novel therapeutic target for neurodegenerative diseases
Fu, T., Chen, X., Zhang, S., Fu, Y., Huang, L., & Xiong, W. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00495 · Cited by 1 · see citing works
Nuclear genetic disorders of mitochondrial DNA gene expression
Glasgow, R. I. C., Lim, A. Z., Nicholls, T. J. J., McFarland, R., Taylor, R. W., & Oláhová, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819656-4.00015-2 · Cited by 1 · see citing works
C6orf203 controls OXPHOS function through modulation of mitochondrial protein biosynthesisPreprint
Palacios-Zambrano, S., Vázquez-Fonseca, L., González-Paramos, C., Mamblona, L., Sánchez‐Caballero, L., Nijtmans, L. G. J., Garesse, R., & Fernández‐Moreno, M. Á. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/704403 · Cited by 1 · see citing works
“described the involvement of C6orf203 in mitochondrial transcription under induced mtDNA depletion and its interaction with mitochondrial RNA polymerase and with TFAM [28], proteins well known to be involved in the synthesis of mtRNAs [48].”
BackgroundThe PPR domain of mitochondrial RNA polymerase is a ribonuclease required for mtDNA replicationPreprint
Liu, Y., Chen, Z., Wang, Z., Delaney, K., Tang, J., Pirooznia, M., Lee, D., Li, Y., & Xu, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.12.435139 · Cited by 1 · see citing works
“However, it is not clear how POLRMT, which transcribes both strands of mtDNA to long polycistronic transcripts (Hillen et al., 2018), can switch from continuous transcription to primer”
BackgroundYazicioglu, Y. F., Marin, E., Sandhu, C., Galiani, S., Raza, I. G. A., Ali, M. A., Kronsteiner, B., Compeer, E. B., Attar, M., Dunachie, S. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.19.500689 · Cited by 1 · see citing works
The mtDNA-derived lncMtDloop promotes mitochondrial homeostasis maintenance and implications in ADPreprint
Xiong, W., Xu, K., Sun, J. K., Liu, S., Zhao, B., Shi, J., Herrup, K., Chow, H., Lü, L., & Li, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.30.564670 · Cited by 1 · see citing works
Cellular metabolic state controls mitochondrial RNA kineticsPreprint
Reardon, S. D., Bautista, C., Cole, S., Cicero, J., & Mishanina, T. V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.13.653903 · Cited by 2 · see citing works
Transcription-dependent phase coexistence of mitochondrial nucleoids and RNA granulesPreprint
Parikh, N., Penna, S. C., Neal, E., & Feric, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.19.694874 · Cited by 1 · see citing works
“For example, mitochondria contain a single mitochondrial RNA polymerase (POLRMT) that transcribes both rRNA and mRNA as long, polycistronic transcripts 30–32 .”
Mitochondrien: wie die Gene im Kraftwerk der Zelle aktiviert werden
Bhatta, A., & Hillen, H. S. (2022) · BIOspektrum · doi:10.1007/s12268-022-1711-z
“ren ein molekulares Bild des Transkriptionszyklus in menschlichen Mitochondrien [8].”
BackgroundInfluentialSelf-citationAge-related decrease in mitochondrial lncMtDloop expression potentiates Alzheimer's pathogenesisPreprint
Xiong, W., Xu, K., Sun, J. K., Liu, S., Zhang, Y., Zhang, Z., Liao, F., Zheng, Y., Shi, J., Herrup, K., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1363630/v1
Yeast mtDNA transcription initiation in single nucleotide addition stepsPreprint
Goovaerts, Q., Shen, J., Wijngaert, B. D., Basu, U., Patel, S. S., & Das, K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.27.509796
Post-transcriptional regulation of genes and mitochondrial disorder
Sabharwal, A., & Kar, B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91305-8.00008-9
Increased mitochondrial transcription initiation does not promote oxidative phosphorylationPreprint
Miranda, M., Mesaros, A., Kuznetsova, I., Purrio, M., Pérard, L., Filipovska, A., Mourier, A., Larsson, N., & Kühl, I. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.11.575236
“Although the basic machinery of mtDNA transcription has been thoroughly studied in vitro (Hillen et al., 2018), little is known about its regulation in vivo .”
BackgroundmtTF1: A Novel Factor Involved in Mitochondrial Gene Expression in Trypanosoma bruceiPreprint
Berger, B. M., Manjunatha, H., Gerber, M., & Ochsenreiter, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.22.655275
“In human mitochondria, for instance, transcription involves four transcription factors (Gustafsson et al., 2016; Hillen et al., 2018).”
- Authors
- Hillen, H. S., Temiakov, D., & Cramer, P.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Thomas Jefferson University (US)
- Corresponding author
- Hillen, Hauke S.
- Cramer, Patrick
- Venue
- Nature Structural & Molecular Biology
- Published
- 2018-09
- Volume
- 25
- Issue
- 9
- Pages
- 754-765
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC6583890
- OpenAlex
- W2890710316
- Cited by
- 111
- References
- 130
- Citations by year
- 2026: 6 · 2025: 22 · 2024: 15 · 2023: 11 · 2022: 19 · 2021: 14 · 2020: 15 · 2019: 8 · 2018: 1
- FWCI
- 0.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- The Medicine Forum (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Boehringer Ingelheim Fonds
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM104231, R01GM118941)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- mitochondrial transcription, mitochondrial RNA polymerase, TFAM, TFB2M, transcription factors, promoter binding, polymerase processivity, human mitochondria
- MeSH terms
- Humans, Mitochondria, Protein Conformation, Terminator Regions, Genetic, Transcription, Genetic, Evolution, Molecular, Mitochondrial Proteins, Transcriptional Elongation Factors
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