ArticleThe Journal of biological chemistry2010
Mitochondrial transcription factor Mtf1 traps the unwound non-template strand to facilitate open complex formation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- The kinetoplastid-specific transcription factor mtTF1 is essential for mitochondrial gene expression and maxicircle replication in Trypanosoma brucei.PLoS biology · 2026Article
- Human mitochondrial RNA polymerase structures reveal transcription start site and slippage mechanism.Molecular cell · 2025Article
- The Identification of the Mitochondrial DNA Polymerase γ (Mip1) of the Entomopathogenic FungusMicroorganisms · 2024Article
- Mitochondrial Transcription of Entomopathogenic Fungi Reveals Evolutionary Aspects of Mitogenomes.Frontiers in microbiology · 2022Article
- Cryo-EM Structures Reveal Transcription Initiation Steps by Yeast Mitochondrial RNA Polymerase.Molecular cell · 2021Article
- Structure, mechanism, and regulation of mitochondrial DNA transcription initiation.The Journal of biological chemistry · 2020Review
- The dynamic landscape of transcription initiation in yeast mitochondria.Nature communications · 2020Article
- The C-terminal tails of the mitochondrial transcription factors Mtf1 and TFB2M are part of an autoinhibitory mechanism that regulates DNA binding.The Journal of biological chemistry · 2020Article
- The C-terminal tail of the yeast mitochondrial transcription factor Mtf1 coordinates template strand alignment, DNA scrunching and timely transition into elongation.Nucleic acids research · 2020Article
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- Human mitochondrial transcription factors TFAM and TFB2M work synergistically in promoter melting during transcription initiation.Nucleic acids research · 2017Article
- Identification of proximal sites for unwound DNA substrate in Escherichia coli topoisomerase I with oxidative crosslinking.FEBS letters · 2017Article
- The thumb subdomain of yeast mitochondrial RNA polymerase is involved in processivity, transcript fidelity and mitochondrial transcription factor binding.RNA biology · 2015Article
- Yeast Mitochondrial Transcription Factor Mtf1 Determines the Precision of Promoter-Directed Initiation of RNA Polymerase Rpo41.PloS one · 2015Article
- Interactions of the yeast mitochondrial RNA polymerase with the +1 and +2 promoter bases dictate transcription initiation efficiency.Nucleic acids research · 2014Article
- Organization of the human mitochondrial transcription initiation complex.Nucleic acids research · 2014Article
- Yeast mitochondrial RNAP conformational changes are regulated by interactions with the mitochondrial transcription factor.Nucleic acids research · 2014Article
- Opening-closing dynamics of the mitochondrial transcription pre-initiation complex.Nucleic acids research · 2012Article
- Transcription factor-dependent DNA bending governs promoter recognition by the mitochondrial RNA polymerase.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The catalytic subunit of the mitochondrial (mt) RNA polymerase (RNAP) is highly homologous to the bacteriophage T7/T3 RNAP. Unlike the phage RNAP, however, the mtRNAP relies on accessory proteins to initiate promoter-specific transcription. Rpo41, the catalytic subunit of the Saccharomyces cerevisiae mtRNAP, requires Mtf1 for opening the duplex promoter. To elucidate the role of Mtf1 in promoter-specific DNA opening, we have mapped the structural organization of the mtRNAP using site-specific protein-DNA photo-cross-linking studies. Both Mtf1 and Rpo41 cross-linked to distinct sites on the promoter DNA, but the dominant cross-links were those of the Mtf1, which indicates a direct role of Mtf1 in promoter-specific binding and initiation. Strikingly, Mtf1 cross-linked with a high efficiency to the melted region of the promoter DNA, based on which we suggest that Mtf1 facilitates DNA melting by trapping the non-template strand in the unwound conformation. Additional strong cross-links of the Mtf1 were observed with the -8 to -10 base-paired region of the promoter. The cross-linking results were incorporated into a structural model of the mtRNAP-DNA, created from a homology model of the C-terminal domain of Rpo41 and the available structure of Mtf1. The promoter DNA is sandwiched between Mtf1 and Rpo41 in the structural model, and Mtf1 closely associates mainly with one face of the promoter across the entire nona-nucleotide consensus sequence. Overall, the studies reveal that in many ways the role of Mtf1 is analogous to the transcription factors of the multisubunit RNAPs, which provides an intriguing link between single- and multisubunit RNAPs.
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