ArticleThe Journal of biological chemistry2010
A dual interface determines the recognition of RNA polymerase II by RNA capping enzyme.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Structures of co-transcriptional RNA capping enzymes on paused transcription complex.Nature communications · 2024Article
- Posttranscriptional Regulation by Proteins and Noncoding RNAs.Advances in experimental medicine and biology · 2024Article
- Interplay of mRNA capping and transcription machineries.Bioscience reports · 2020Review
- The capping enzyme facilitates promoter escape and assembly of a follow-on preinitiation complex for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- CTD-dependent and -independent mechanisms govern co-transcriptional capping of Pol II transcripts.Nature communications · 2018Article
- Review
- Article
- The RNAs of RNA-directed DNA methylation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2017Review
- The evolutionarily conserved Pol II flap loop contributes to proper transcription termination on short yeast genes.Cell reports · 2014Article
- Coupling mRNA processing with transcription in time and space.Nature reviews. Genetics · 2014Review
- Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Molecules (Basel, Switzerland) · 2014Review
- Putting an 'End' to HIV mRNAs: capping and polyadenylation as potential therapeutic targets.AIDS research and therapy · 2013Article
- RNA polymerase II transcription elongation control.Chemical reviews · 2013Review
- The C-terminal domain of Rpb1 functions on other RNA polymerase II subunits.Molecular cell · 2013Article
- Correct assembly of RNA polymerase II depends on the foot domain and is required for multiple steps of transcription in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
- High-throughput genetic and gene expression analysis of the RNAPII-CTD reveals unexpected connections to SRB10/CDK8.PLoS genetics · 2013Article
- The Spt4-Spt5 complex: a multi-faceted regulator of transcription elongation.Biochimica et biophysica acta · 2013Review
- The RNA polymerase II CTD coordinates transcription and RNA processing.Genes & development · 2012Review
- Regulation of mammalian transcription by Gdown1 through a novel steric crosstalk revealed by cryo-EM.The EMBO journal · 2012Article
- The conserved foot domain of RNA pol II associates with proteins involved in transcriptional initiation and/or early elongation.Genetics · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
RNA capping enzyme (CE) is recruited specifically to RNA polymerase II (Pol II) transcription sites to facilitate cotranscriptional 5'-capping of pre-mRNA and other Pol II transcripts. The current model to explain this specific recruitment of CE to Pol II as opposed to Pol I and Pol III rests on the interaction between CE and the phosphorylated C-terminal domain (CTD) of Pol II largest subunit Rpb1 and more specifically between the CE nucleotidyltransferase domain and the phosphorylated CTD. Through biochemical and diffraction analyses, we demonstrate the existence of a distinctive stoichiometric complex between CE and the phosphorylated Pol II (Pol IIO). Analysis of the complex revealed an additional and unexpected polymerase-CE interface (PCI) located on the multihelical Foot domain of Rpb1. We name this interface PCI1 and the previously known nucleotidyltransferase/phosphorylated CTD interface PCI2. Although PCI1 and PCI2 individually contribute to only weak interactions with CE, a dramatically stabilized and stoichiometric complex is formed when PCI1 and PCI2 are combined in cis as they occur in an intact phosphorylated Pol II molecule. Disrupting either PCI1 or PCI2 by alanine substitution or deletion diminishes CE association with Pol II and causes severe growth defects in vivo. Evidence from manipulating PCI1 indicates that the Foot domain contributes to the specificity in CE interaction with Pol II as opposed to Pol I and Pol III. Our results indicate that the dual interface based on combining PCI1 and PCI2 is required for directing CE to Pol II elongation complexes.
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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.