ArticleThe Journal of biological chemistry2009
A promoter recognition mechanism common to yeast mitochondrial and phage t7 RNA polymerases.
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. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
- Mechanisms of mitochondrial promoter recognition in humans and other mammalian species.Nucleic acids research · 2022Article
- Cryo-EM Structures Reveal Transcription Initiation Steps by Yeast Mitochondrial RNA Polymerase.Molecular cell · 2021Article
- The dynamic landscape of transcription initiation in yeast mitochondria.Nature communications · 2020Article
- Promoter Length Affects the Initiation of T7 RNA Polymerase In Vitro: New Insights into Promoter/Polymerase Co-evolution.Journal of molecular evolution · 2020Article
- Structural basis of mitochondrial transcription.Nature structural & molecular biology · 2018Review
- Mitochondrial transcription in mammalian cells.Frontiers in bioscience (Landmark edition) · 2017Review
- In vitro promoter recognition by the catalytic subunit of plant phage-type RNA polymerases.Plant molecular biology · 2016Article
- A model for transcription initiation in human mitochondria.Nucleic acids research · 2015Article
- 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
- Yeast mitochondrial RNAP conformational changes are regulated by interactions with the mitochondrial transcription factor.Nucleic acids research · 2014Article
- Structure of human mitochondrial RNA polymerase elongation complex.Nature structural & molecular biology · 2013Article
- Conservation of promoter melting mechanisms in divergent regions of the single-subunit RNA polymerases.Biochemistry · 2012Article
- The manner in which DNA is packaged with TFAM has an impact on transcription activation and inhibition.FEBS open bio · 2012Article
- Structure of human mitochondrial RNA polymerase.Nature · 2011Article
- The N-terminal domain of the yeast mitochondrial RNA polymerase regulates multiple steps of transcription.The Journal of biological chemistry · 2011Article
- Identification of multiple rate-limiting steps during the human mitochondrial transcription cycle in vitro.The Journal of biological chemistry · 2010Article
- Multiple functions of yeast mitochondrial transcription factor Mtf1p during initiation.The Journal of biological chemistry · 2010Article
- Mitochondrial transcription factor Mtf1 traps the unwound non-template strand to facilitate open complex formation.The Journal of biological chemistry · 2010Article
- Mechanism of transcription initiation by the yeast mitochondrial RNA polymerase.Biochimica et biophysica actaReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Yeast mitochondrial (YMt) and phage T7 RNA polymerases (RNAPs) are two divergent representatives of a large family of single subunit RNAPs that are also found in the mitochondria and chloroplasts of higher eukaryotes, mammalian nuclei, and many other bacteriophage. YMt and phage T7 promoters differ greatly in sequence and length, and the YMt RNAP uses an accessory factor for initiation, whereas T7 RNAP does not. We obtain evidence here that, despite these apparent differences, both the YMt and T7 RNAPs utilize a similar promoter recognition loop to bind their respective promoters. Mutations in this element in YMt RNAP specifically disrupt mitochondrial promoter utilization, and experiments with site-specifically tethered chemical nucleases indicate that this element binds the mitochondrial promoter almost identically to how the promoter recognition loop from the phage RNAP binds its promoter. Sequence comparisons reveal that the other members of the single subunit RNAP family display loops of variable sequence and size at a position corresponding to the YMt and T7 RNAP promoter recognition loops. We speculate that these elements may be involved in promoter recognition in most or all of these enzymes and that this element's structure allows it to accommodate significant sequence and length variation to provide a mechanism for rapid evolution of new promoter specificities in this RNAP family.
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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.