ArticleProceedings of the National Academy of Sciences of the United States of America2011
X-ray crystal structures elucidate the nucleotidyl transfer reaction of transcript initiation using two nucleotides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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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25 citing papers in PubMed, 39 citations in OpenAlex.
- Cryo-EM study of bacteriophage N4 virion RNA polymerase.Journal of bacteriology · 2026Article
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- Structural basis for substrate binding and selection by human mitochondrial RNA polymerase.Nature communications · 2024Article
- Quantitative analysis of transcription start site selection reveals control by DNA sequence, RNA polymerase II activity and NTP levels.Nature structural & molecular biology · 2024Article
- On the Recognition of Natural Substrate CTP and Endogenous Inhibitor ddhCTP of SARS-CoV-2 RNA-Dependent RNA Polymerase: A Molecular Dynamics Study.Journal of chemical information and modeling · 2022Article
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Promoter-sequence determinants and structural basis of primer-dependent transcription initiation inProceedings of the National Academy of Sciences of the United States of America · 2021Article
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- Allosteric activation of SARS-CoV-2 RdRp by remdesivir triphosphate and other phosphorylated nucleotides.bioRxiv : the preprint server for biology · 2021Article
- The mechanism of the nucleo-sugar selection by multi-subunit RNA polymerases.Nature communications · 2021Article
- Watching the bacterial RNA polymerase transcription reaction by time-dependent soak-trigger-freeze X-ray crystallography.The Enzymes · 2021Review
- TheMicroorganisms · 2020Article
- Article
- Universal promoter scanning by Pol II during transcription initiation in Saccharomyces cerevisiae.Genome biology · 2020Article
- Quantifying the RNA cap epitranscriptome reveals novel caps in cellular and viral RNA.Nucleic acids research · 2019Article
- Pervasive and dynamic transcription initiation inGenome research · 2019Article
- Genome-wide effects onProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structures of a DNA Polymerase Inserting Therapeutic Nucleotide Analogues.Chemical research in toxicology · 2017Article
- Structural and biochemical investigation of bacteriophage N4-encoded RNA polymerases.Biomolecules · 2015Review
- Relationships of RNA polymerase II genetic interactors to transcription start site usage defects and growth in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2014Article
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5 authors at 2 institutions in 1 country.
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Abstract
We have determined the X-ray crystal structures of the pre- and postcatalytic forms of the initiation complex of bacteriophage N4 RNA polymerase that provide the complete set of atomic images depicting the process of transcript initiation by a single-subunit RNA polymerase. As observed during T7 RNA polymerase transcript elongation, substrate loading for the initiation process also drives a conformational change of the O-helix, but only the correct base pairing between the +2 substrate and DNA base is able to complete the O-helix conformational transition. Substrate binding also facilitates catalytic metal binding that leads to alignment of the reactive groups of substrates for the nucleotidyl transfer reaction. Although all nucleic acid polymerases use two divalent metals for catalysis, they differ in the requirements and the timing of binding of each metal. In the case of bacteriophage RNA polymerase, we propose that catalytic metal binding is the last step before the nucleotidyl transfer reaction.
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