ArticleBiochimica et biophysica acta. Proteins and proteomics2024
Protein interaction network revealed by quantitative proteomic analysis links TFIIB to multiple aspects of the transcription cycle.
Article in Biochimica et biophysica acta. Proteins and proteomics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Cleavage of the RNA polymerase II general transcription factor TFIIB tunes transcription during stress.Genes & development · 2026Article
- Protein-interaction network analysis reveals the role of Prp19 splicing factor in transcription of both intron-containing and intron-lacking genes.PLoS genetics · 2026Article
- idopNetwork Analysis of Salt-Responsive Transcriptomes Reveals Hub Regulatory Modules and Genes inInternational journal of molecular sciences · 2025Article
- The Central FacilitaTOR: Coordinating Transcription and Translation in Eukaryotes.International journal of molecular sciences · 2025Review
- TFIIB-Termination Factor Interaction Affects Termination of Transcription on Genome-Wide Scale.International journal of molecular sciences · 2024Article
- Genome-wide analysis of TFIIB's role in termination of transcription.Research square · 2024Article
- Sub2: A TFIIB Interacting Protein with Pleiotropic Roles in mRNA Synthesis, Processing and Transport.International journal of biochemistry & physiology · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Although TFIIB is widely regarded as an initiation factor, recent reports have implicated it in multiple aspects of eukaryotic transcription. To investigate the broader role of TFIIB in transcription, we performed quantitative proteomic analysis of yeast TFIIB. We purified two different populations of TFIIB; one from soluble cell lysate, which is not engaged in transcription, and the other from the chromatin fraction which yields the transcriptionally active form of the protein. TFIIB purified from the chromatin exhibits several interactions that explain its non-canonical roles in transcription. RNAPII, TFIIF and TFIIH were the only components of the preinitiation complex with a significant presence in chromatin TFIIB. A notable feature was enrichment of all subunits of CF1 and Rat1 3' end processing-termination complexes in chromatin-TFIIB preparation. Subunits of the CPF termination complex were also detected in both chromatin and soluble derived TFIIB preparations. These results may explain the presence of TFIIB at the 3' end of genes during transcription as well as its role in promoter-termination interaction.
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