ArticleProceedings of the National Academy of Sciences of the United States of America2021
Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- Nup42 safeguards heat-induced mRNAs from nuclear condensation to support chaperone synthesis.bioRxiv : the preprint server for biology · 2026Article
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025Article
- Cryo-EM structure of the CBC-ALYREF complex.eLife · 2024Article
- Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly.Cell reports · 2023Article
- Article
- Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2.eLife · 2021Article
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8 authors.
Funding
Abstract
The C-terminal domain (CTD) kinase I (CTDK-1) complex is the primary RNA Polymerase II (Pol II) CTD Ser2 kinase in budding yeast. CTDK-1 consists of a cyclin-dependent kinase (CDK) Ctk1, a cyclin Ctk2, and a unique subunit Ctk3 required for CTDK-1 activity. Here, we present a crystal structure of CTDK-1 at 1.85-Å resolution. The structure reveals that, compared to the canonical two-component CDK-cyclin system, the third component Ctk3 of CTDK-1 plays a critical role in Ctk1 activation by stabilizing a key element of CDK regulation, the T-loop, in an active conformation. In addition, Ctk3 contributes to the assembly of CTDK-1 through extensive interactions with both Ctk1 and Ctk2. We also demonstrate that CTDK-1 physically and genetically interacts with the serine/arginine-like protein Gbp2. Together, the data in our work reveal a regulatory mechanism of CDK complexes.
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