ArticleThe Journal of biological chemistry2009
Fluorescence mapping of the open complex of yeast mitochondrial RNA polymerase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Human mitochondrial RNA polymerase structures reveal transcription start site and slippage mechanism.Molecular cell · 2025Article
- Article
- Assembly and Cryo-EM structure determination of yeast mitochondrial RNA polymerase initiation complex intermediates.STAR protocols · 2021Article
- 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
- Article
- Transcriptional fidelities of human mitochondrial POLRMT, yeast mitochondrial Rpo41, and phage T7 single-subunit RNA polymerases.The Journal of biological chemistry · 2017Article
- Human mitochondrial transcription factors TFAM and TFB2M work synergistically in promoter melting during transcription initiation.Nucleic acids research · 2017Article
- The Yeast Mitochondrial RNA Polymerase and Transcription Factor Complex Catalyzes Efficient Priming of DNA Synthesis on Single-stranded DNA.The Journal of biological chemistry · 2016Article
- 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
- Article
- 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
- Fluorescent DNA-based enzyme sensors.Chemical Society reviews · 2011Review
- Transcription factor-dependent DNA bending governs promoter recognition by the mitochondrial RNA polymerase.The Journal of biological chemistry · 2011Article
- Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe.Nucleic acids research · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
The mitochondrial RNA polymerase (mtRNAP) of Saccharomyces cerevisiae, consisting of a complex of Rpo41 and Mtf1, is homologous to the phage single polypeptide T7/T3 RNA polymerases. The yeast mtRNAP recognizes a conserved nonanucleotide sequence to initiate specific transcription. In this work, we have defined the region of the nonanucleotide that is melted by the mtRNAP using 2-aminopurine (2AP) fluorescence that is sensitive to changes in base stacking interactions. We show that mtRNAP spontaneously melts the promoter from -4 to +2 forming a bubble around the transcription start site at +1. The location and size of the DNA bubble in this open complex of the mtRNAP closely resembles that of the T7 RNA polymerase. We show that DNA melting requires the simultaneous presence of Rpo41 and Mtf1. Adding the initiating nucleotide ATP does not expand the size of the initially melted DNA, but the initiating nucleotide differentially affects base stacking interactions at -1 and -2. Thus, the promoter structure upstream of the transcription start site is slightly rearranged during early initiation from its structure in the pre-initiation stage. Unlike on the duplex promoter, Rpo41 alone was able to form a competent open complex on a pre-melted promoter. The results indicate that Rpo41 contains the elements for recognizing the melted promoter through interactions with the template strand. We propose that Mtf1 plays a role in base pair disruption during the early stages of open complex formation.
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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.