Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.
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TLDR
The highly conserved C-terminal domain (CTD) of the largest subunit of RNA polymerase II comprises a consensus heptad (Y1S2P3T4S5P6S7) repeated multiple times as mentioned in this paper.About:
This article is published in Journal of Molecular Biology.The article was published on 2021-03-04 and is currently open access. It has received 8 citations till now. The article focuses on the topics: RNA polymerase II & Eukaryotic transcription.read more
Citations
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Journal ArticleDOI
Decoding Post-Translational Modification Crosstalk With Proteomics.
TL;DR: In this paper, the authors provide an overview of the basic modes of PTM crosstalk, the proteomic methods to elucidate PTM co-stalk and approaches that can inform about the functional consequences.
Journal ArticleDOI
Live imaging of transcription sites using an elongating RNA polymerase II-specific probe.
Satoshi Uchino,Yuma Ito,Yuko Sato,Tetsuya Handa,Yasuyuki Ohkawa,Makio Tokunaga,Hiroshi Kimura +6 more
TL;DR: In this paper, a modified Intacellular Antibilinear Antibody (mintbody) was used to detect the sites of RNAP2 Ser2ph-mintbody foci.
Journal ArticleDOI
What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domain via mass spectrometry.
Blase M LeBlanc,R Yvette Moreno,Edwin E. Escobar,Mukesh Kumar Venkat Ramani,Jennifer S. Brodbelt,Yan Zhang +5 more
TL;DR: The development of various MS techniques are discussed and the pros and cons of each technique are highlighted to provide future investigators with a comprehensive overview of how MS can be used to investigate the complexities of RNAP-II mediated transcription.
Journal ArticleDOI
Evaluating Spatiotemporal Dynamics of Phosphorylation of RNA Polymerase II Carboxy-Terminal Domain by Ultraviolet Photodissociation Mass Spectrometry.
TL;DR: In this paper, a quantitative parallel reaction monitoring (PRM) method was developed to monitor spatiotemporal changes in site-specific Ser5 phosphorylation of the carboxyl-terminal domain (CTD) by cyclin-dependent kinase 7 (CDK7) using UVPD for sequence identification, phosphosite localization, and differentiation of phosphopeptide isomers.
Posted ContentDOI
Visualizing transcription sites in living cells using a genetically encoded probe specific for the elongating form of RNA polymerase II
Satoshi Uchino,Yuma Ito,Yuko Sato,Tetsuya Handa,Yasuyuki Ohkawa,Makio Tokunaga,Hiroshi Kimura +6 more
TL;DR: In this paper, the authors developed a modification-specific Intacellular Antibody (mintbody) probe to detect the Ser2- phosphorylated, elongating form of RNA Polymerase II in living cells.
References
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Journal ArticleDOI
Structural Insights to How Mammalian Capping Enzyme Reads the CTD Code
TL;DR: The crystal structure of the RNA guanylyltransferase component of mammalian capping enzyme (Mce) bound to a CTD phosphopeptide is reported, showing an extended β-like conformation that docks Tyr1 and Ser5-PO(4) onto the Mce nucleotidyltransferase domain.
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Direct Analysis of Phosphorylation Sites on the Rpb1 C-Terminal Domain of RNA Polymerase II.
TL;DR: It is shown that Ser5-P and Ser2-P occur throughout the length of CTD and are far more abundant than other phosphorylation sites and suggest a relatively sparse and simple "CTD code".
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Activated transcription independent of the RNA polymerase II holoenzyme in budding yeast
TL;DR: The Pol II holoenzyme is not essential for all UAS-dependent activated transcription in yeast, and the upstream-activating sequence of the CUP1 promoter was sufficient to drive Cu2+ inducible transcription without Srb4 and heat shock inducibly transcription without the CTD.
Journal ArticleDOI
Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription.
TL;DR: In this paper, the Set2 SRI domain of the histone H3 methyltransferase Set2 was shown to have a left-handed three-helix bundle, which resembles the structure of an RNA polymerase-interacting domain in bacterial σ factors.
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Structural basis of an essential interaction between influenza polymerase and Pol II CTD
Maria Lukarska,Guillaume Fournier,Guillaume Fournier,Guillaume Fournier,Alexander Pflug,Patricia Resa-Infante,Stefan Reich,Nadia Naffakh,Nadia Naffakh,Nadia Naffakh,Stephen Cusack +10 more
TL;DR: It is concluded that direct binding of FluPol to the SeP5 Pol II CTD is fine-tuned to allow efficient viral transcription and proposed that the CTD-binding site on FluPol could be targeted for antiviral drug development.