ArticleMolecular and cellular biology2005
Role of the mammalian RNA polymerase II C-terminal domain (CTD) nonconsensus repeats in CTD stability and cell proliferation.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 56 citations in OpenAlex.
- RNA polymerase II phosphorylation dynamics: from molecular mechanisms to human disease.RNA biology · 2026Review
- RNA polymerase II CTD is dispensable for transcription and required for termination in human cells.EMBO reports · 2023Article
- Germline mutation inHGG advances · 2021Article
- Extension of the minimal functional unit of the RNA polymerase II CTD from yeast to mammalian cells.Biology letters · 2019Article
- Genetic analysis of the RNA polymerase II CTD in Drosophila.Methods (San Diego, Calif.) · 2019Review
- Analysis of RNA polymerase II ubiquitylation and proteasomal degradation.Methods (San Diego, Calif.) · 2019Article
- The C-Terminal Domain of RNA Polymerase II Is a Multivalent Targeting Sequence that Supports Drosophila Development with Only Consensus Heptads.Molecular cell · 2019Article
- Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain.Nature communications · 2017Article
- Specific threonine-4 phosphorylation and function of RNA polymerase II CTD during M phase progression.Scientific reports · 2016Article
- A single flexible RNAPII-CTD integrates many different transcriptional programs.Transcription · 2016Article
- Methylation of RNA polymerase II non-consensus Lysine residues marks early transcription in mammalian cells.eLife · 2015Article
- Evolution of lysine acetylation in the RNA polymerase II C-terminal domain.BMC evolutionary biology · 2015Article
- Site-specific methylation and acetylation of lysine residues in the C-terminal domain (CTD) of RNA polymerase II.Transcription · 2015Article
- Function and control of RNA polymerase II C-terminal domain phosphorylation in vertebrate transcription and RNA processing.Molecular and cellular biology · 2014Article
- Article
- Evolutionary diversity and taxon-specific modifications of the RNA polymerase II C-terminal domain.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Molecules (Basel, Switzerland) · 2014Review
- RNA polymerase II C-terminal domain: Tethering transcription to transcript and template.Chemical reviews · 2013Review
- Acetylation of RNA polymerase II regulates growth-factor-induced gene transcription in mammalian cells.Molecular cell · 2013Article
- Histone methyltransferase SETD2 coordinates FACT recruitment with nucleosome dynamics during transcription.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C-terminal domain (CTD) of mammalian RNA polymerase II (Pol II) consists of 52 repeats of the consensus heptapeptide YSPTSPS and links transcription to the processing of pre-mRNA. The length of the CTD and the number of repeats diverging from the consensus sequence have increased through evolution, but their functional importance remains unknown. Here, we show that the deletion of repeats 1 to 3 or 52 leads to cleavage and degradation of the CTD from Pol II in vivo. Including these repeats, however, allowed the construction of stable, synthetic CTDs. To our surprise, polymerases consisting of just consensus repeats could support normal growth and viability of cells. We conclude that all other nonconsensus CTD repeats are dispensable for the transcription and pre-mRNA processing of genes essential for proliferation.
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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.