ArticleProtein expression and purification2010
Improved methods for expression and purification of Saccharomyces cerevisiae TFIIF and TFIIH; identification of a functional Escherichia coli promoter and internal translation initiation within the N-terminal coding region of the TFIIF TFG1 subunit.
Article in Protein expression and purification, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- In vitro reconstitution of yeast RNA polymerase II transcription initiation with high efficiency.Methods (San Diego, Calif.) · 2019Article
- Article
- Transcription factors IIS and IIF enhance transcription efficiency by differentially modifying RNA polymerase pausing dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Evidence that RNA polymerase II and not TFIIB is responsible for the difference in transcription initiation patterns between Saccharomyces cerevisiae and Schizosaccharomyces pombe.Nucleic acids research · 2012Article
- Control of the function of the transcription and repair factor TFIIH by the action of the cochaperone Ydj1.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex.The EMBO journal · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The basal RNA polymerase II (RNAPII) transcription machinery is composed of RNAPII and the general transcription factors (TF) TATA binding protein (TBP), TFIIB, TFIIE, TFIIF and TFIIH. Due to the powerful genetic and molecular approaches that can be utilized, the budding yeast Saccharomyces cerevisiae has proven to be an invaluable model system for studies of the mechanisms of RNAPII transcription. Complementary biochemical studies of the S. cerevisiae basal transcription machinery, however, have been hampered by difficulties in the purification of TFIIF and TFIIH, most notably due to the severe toxicity of the TFIIF Tfg1 subunit in Escherichia coli and the complexity of the purification scheme for native TFIIH. Here, we report the elimination of TFG1-associated toxicity in E. coli, the identification and removal of a functional E. coli promoter and internal translation initiation within the N-terminal coding region of TFG1, and the efficient production and two-step purification of recombinant TFIIF complexes. We also report conditions for the efficient two-step tandem affinity purification (TAP) of holo-TFIIH, core TFIIH and TFIIK complexes from yeast whole cell extracts.
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