ArticleACS chemical biology2020
Structural Motifs for CTD Kinase Specificity on RNA Polymerase II during Eukaryotic Transcription.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Communication is key: combinatorial phosphorylation and functional cross-talk in the RNA polymerase II CTD code.Biochemical Society transactions · 2026Review
- Kaposi's Sarcoma-associated herpesvirus uses a novel protein fold to hijack RNA Polymerase II for viral late gene transcription.bioRxiv : the preprint server for biology · 2026Article
- A tunable CTD grammar governs the spatial programming of the transcription cycle.Nature communications · 2026Article
- Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription.Nature communications · 2024Article
- Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription.bioRxiv : the preprint server for biology · 2024Article
- Distinctive interactomes of RNA polymerase II phosphorylation during different stages of transcription.iScience · 2023Article
- PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC.Nature communications · 2021Article
- What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domainRSC chemical biology · 2021Review
- Evaluating Spatiotemporal Dynamics of Phosphorylation of RNA Polymerase II Carboxy-Terminal Domain by Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Chemical Society · 2021Article
- Collaborators or competitors: the communication between RNA polymerase II and the nucleosome during eukaryotic transcription.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
The phosphorylation states of RNA polymerase II coordinate the process of eukaryotic transcription by recruitment of transcription regulators. The individual residues of the repetitive heptad of the C-terminal domain (CTD) of the biggest subunit of RNA polymerase II are phosphorylated temporally at different stages of transcription. Intriguingly, despite similar flanking residues, phosphorylation of Ser2 and Ser5 in CTD heptads play dramatically different roles. The mechanism of how the kinases place phosphorylation on the correct serine is not well understood. In this paper, we use biochemical assays, mass spectrometry, molecular modeling, and structural analysis to understand the structural elements determining which serine of the CTD heptad is subject to phosphorylation. We identified three motifs in the activation/P+1 loops differentiating the intrinsic specificity of CTD in various CTD kinases. We characterized the enzyme specificity of the CTD kinases-CDK7 as Ser5-specific, Erk2 with dual specificity for Ser2 and Ser5, and Dyrk1a as a Ser2-specific kinase. We also show that the specificities of kinases are malleable and can be modified by incorporating mutations in their activation/P+1 loops that alter the interactions of the three motifs. Our results provide an important clue to the understanding of post-translational modification of RNA polymerase II temporally during active transcription.
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