ArticleScience (New York, N.Y.)2011
Initiation complex structure and promoter proofreading.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed.
- The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026Review
- Mechanism of mammalian transcriptional repression by noncoding RNA.Nature structural & molecular biology · 2025Article
- Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II.Molecular cell · 2022Article
- Cryo-EM Structures Reveal Transcription Initiation Steps by Yeast Mitochondrial RNA Polymerase.Molecular cell · 2021Article
- Nucleosomal proofreading of activator-promoter interactions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mechanisms of Transcriptional Pausing in Bacteria.Journal of molecular biology · 2019Review
- Transcription preinitiation complex structure and dynamics provide insight into genetic diseases.Nature structural & molecular biology · 2019Article
- Histone Marks in the 'Driver's Seat': Functional Roles in Steering the Transcription Cycle.Trends in biochemical sciences · 2017Review
- Multisubunit DNA-Dependent RNA Polymerases from Vaccinia Virus and Other Nucleocytoplasmic Large-DNA Viruses: Impressions from the Age of Structure.Microbiology and molecular biology reviews : MMBR · 2017Review
- Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- The elongation factor Spt5 facilitates transcription initiation for rapid induction of inflammatory-response genes.Nature communications · 2016Article
- Mechanism of Concerted RNA-DNA Primer Synthesis by the Human Primosome.The Journal of biological chemistry · 2016Article
- Structures of E. coli σS-transcription initiation complexes provide new insights into polymerase mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Characterization of the Saccharomyces cerevisiae ATP-Interactome using the iTRAQ-SPROX Technique.Journal of the American Society for Mass Spectrometry · 2016Article
- Crystal Structure of a Transcribing RNA Polymerase II Complex Reveals a Complete Transcription Bubble.Molecular cell · 2015Article
- Structural Model of RNA Polymerase II Elongation Complex with Complete Transcription Bubble Reveals NTP Entry Routes.PLoS computational biology · 2015Article
- Crystal structures of the E. coli transcription initiation complexes with a complete bubble.Molecular cell · 2015Article
- Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme.The Journal of biological chemistry · 2014Article
- Millisecond dynamics of RNA polymerase II translocation at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The initiation of transcription by RNA polymerase II is a multistage process. X-ray crystal structures of transcription complexes containing short RNAs reveal three structural states: one with 2- and 3-nucleotide RNAs, in which only the 3'-end of the RNA is detectable; a second state with 4- and 5-nucleotide RNAs, with an RNA-DNA hybrid in a grossly distorted conformation; and a third state with RNAs of 6 nucleotides and longer, essentially the same as a stable elongating complex. The transition from the first to the second state correlates with a markedly reduced frequency of abortive initiation. The transition from the second to the third state correlates with partial "bubble collapse" and promoter escape. Polymerase structure is permissive for abortive initiation, thereby setting a lower limit on polymerase-promoter complex lifetime and allowing the dissociation of nonspecific complexes. Abortive initiation may be viewed as promoter proofreading, and the structural transitions as checkpoints for promoter control.
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Registered trials
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.