ArticleScience advances2021
Structure of TFIIK for phosphorylation of CTD of RNA polymerase II.
Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026Review
- Article
- Review
- Transcription start site scanning requires the fungi-specific hydrophobic loop of Tfb3.Nucleic acids research · 2024Article
- Structures and compositional dynamics of Mediator in transcription regulation.Current opinion in structural biology · 2024Review
- Structural basis of Cdk7 activation by dual T-loop phosphorylation.Nature communications · 2024Article
- Structural basis of Cdk7 activation by dual T-loop phosphorylation.bioRxiv : the preprint server for biology · 2024Article
- TopEnzyme: a framework and database for structural coverage of the functional enzyme space.Bioinformatics (Oxford, England) · 2023Article
- Structural basis of a transcription pre-initiation complex on a divergent promoter.Molecular cell · 2023Article
- Unveiling the noncanonical activation mechanism of CDKs: insights from recent structural studies.Frontiers in molecular biosciences · 2023Review
- Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II.Molecular cell · 2022Article
- Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair.Nature communications · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive modifications coupled to transcription elongation, mRNA processing, and histone dynamics. We have determined a 3.5-Å resolution cryo-electron microscopy (cryo-EM) structure of the TFIIH kinase module (TFIIK in yeast), which is composed of Kin28, Ccl1, and Tfb3, yeast homologs of CDK7, cyclin H, and MAT1, respectively. The carboxyl-terminal region of Tfb3 was lying at the edge of catalytic cleft of Kin28, where a conserved Tfb3 helix served to stabilize the activation loop in its active conformation. By combining the structure of TFIIK with the previous cryo-EM structure of the preinitiation complex, we extend the previously proposed model of the CTD path to the active site of TFIIK.
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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.